Means for treating myosin-related diseases

ABSTRACT

The present invention provides a method of designing a modulator of a myosin, the method comprising molecular modeling of a compound such that the modeled compound interacts with at least three amino acid residues of said myosin, said residues being selected from (a) ranges K265-V268, V411-L441, N588-Q593, D614-T629, and V630-E646 of SEQ ID NO: 2, said myosin comprising or consisting of (i) the sequence of SEQ ID NO: 2; (ii) the sequence encoded by the sequence of SEQ ID NO: 1; (iii) a sequence being at least 40% identical to the sequence of SEQ ID NO: 2 or to the sequence encoded by the sequence of SEQ ID NO: 1; or (iv) a sequence encoded by a sequence being at least 40% identical to the sequence of SEQ ID NO: 1; wherein said sequence of (iii) or (iv) comprises said three amino acid residues, and wherein said residues comprise K265; or (b) ranges of any one of SEQ ID NOs: 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, 80, 82, 84, 86, 88, 90, 92, 94, 96, 98, 100, 102, 104, 106 or 108, respectively, said ranges aligning with the ranges of SEQ ID NO: 2 as defined in (a), said myosin comprising or consisting of (i) the sequence of any one of SEQ ID NO: 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, 80, 82, 84, 86, 88, 90, 92, 94, 96, 98, 100, 102, 104, 106 or 108, respectively; (ii) the sequence encoded by the sequence of any one of SEQ ID NO: 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, 47, 49, 51, 53, 55, 57, 59, 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, 81, 83, 85, 87, 89, 91, 93, 95, 97, 99, 101, 103, 105, 107 or 109; respectively; (iii) a sequence being at least 40% identical to the sequence of any one of SEQ ID NO: 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, 80, 82, 84, 86, 88, 90, 92, 94, 96, 98, 100, 102, 104, 106 or 108, respectively, or to the sequence encoded by the sequence of any one of SEQ ID NO: 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, 47, 49, 51, 53, 55, 57, 59, 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, 81, 83, 85, 87, 89, 91, 93, 95, 97, 99, 101, 103, 105, 107 or 109, respectively; or (iv) a sequence encoded by a sequence being at least 40% identical to the sequence of any one of SEQ ID NO: 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, 47, 49, 51, 53, 55, 57, 59, 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, 81, 83, 85, 87, 89, 91, 93, 95, 97, 99, 101, 103, 105, 107 or 109, respectively; wherein said sequence of (iii) or (iv) comprises said three amino acid residues, and wherein said residues comprise the residue aligning with K265 of SEQ ID NO: 2; thereby obtaining said modulator of a myosin. Furthermore provided are a method of identifying a modulator of a myosin, pharmaceutical compositions and methods of treating cardiovascular diseases, cancer, diseases of the central nervous system, viral infections, and infections by parasites of the Apicomplexa family.

This invention relates to a method of designing a modulator of a myosin, the method comprising molecular modeling of a compound such that the modeled compound interacts with at least three amino acid residues of said myosin, said residues being selected from (a) ranges K265-V268, V411-L441, N588-Q593, D614-T629, and V630-E646 of SEQ ID NO: 2, said myosin comprising or consisting of (i) the sequence of SEQ ID NO: 2; (ii) the sequence encoded by the sequence of SEQ ID NO: 1; (iii) a sequence being at least 40% identical to the sequence of SEQ ID NO: 2 or to the sequence encoded by the sequence of SEQ ID NO: 1; or (iv) a sequence encoded by a sequence being at least 40% identical to the sequence of SEQ ID NO: 1; wherein said sequence of (iii) or (iv) comprises said three amino acid residues, and wherein said residues comprise K265; or (b) ranges of any one of SEQ ID NOs: 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, 80, 82, 84, 86, 88, 90, 92, 94, 96, 98, 100, 102, 104, 106 or 108, respectively, said ranges aligning with the ranges of SEQ ID NO: 2 as defined in (a), said myosin comprising or consisting of (i) the sequence of any one of SEQ ID. NO: 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, 80, 82, 84, 86, 88, 90, 92, 94, 96, 98, 100, 102, 104, 106 or 108, respectively; (ii) the sequence encoded by the sequence of any one of SEQ ID NO: 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, 47, 49, 51, 53, 55, 57, 59, 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, 81, 83, 85, 87, 89, 91, 93, 95, 97, 99, 101, 103, 105, 107 or 109, respectively; (iii) a sequence being at least 40% identical to the sequence of any one of SEQ ID NO: 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, 80, 82, 84, 86, 88, 90, 92, 94, 96, 98, 100, 102, 104, 106 or 108, respectively, or to the sequence encoded by the sequence of any one of SEQ ID NO: 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, 47, 49, 51, 53, 55, 57, 59, 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, 81, 83, 85, 87, 89, 91, 93, 95, 97, 99, 101, 103, 105, 107 or 109, respectively; or (iv) a sequence encoded by a sequence being at least 40% identical to the sequence of any one of SEQ ID NO: 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, 47, 49, 51, 53, 55, 57, 59, 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, 81, 83, 85, 87, 89, 91, 93, 95, 97, 99, 101, 103, 105, 107 or 109, respectively; wherein said sequence of (iii) or (iv) comprises said three amino acid residues, and wherein said residues comprise the residue aligning with K265 of SEQ ID NO: 2; thereby obtaining said modulator of a myosin.

In this specification, a number of documents including patent applications and manufacturer's manuals are cited. The disclosure of these documents, while not considered relevant for the patentability of this invention, is herewith incorporated by reference in its entirety.

Myosins are motor proteins which are involved in a large number of motility processes. By decomposing, more specifically hydrolysing ATP, myosins generate a directed force which permits movement along actin filaments. Known myosin-dependent processes include muscle contraction, cell division, movements of entire cells, intracellular transport of organelles and vesicles, endocytosis as well as maintenance and modification of actin-rich structures such as the cytoskeleton.

Cellular motility as well as aberrant forms thereof are involved in numerous diseases and conditions including cardiovascular diseases, cancer, malaria, and diseases of the central nervous system. Known inhibitors of myosin such as Blebbistatin (Kovacs M, Toth J, Hetenyi C, Malnasi-Csizmadia A, Sellers J R. J. Biol. Chem. 2004, 279: 35557-35563), BDM (2,3-butanedione monoxime) and BTS (N-benzyl-p-toluol-sulfonamide) (Cheung A, Dantzig J A, Hollingworth S, Baylor S M, Goldman Y E, Mitchison T J, Straight A F. Nat. Cell Biol. 2002, 4: 83:8) lend themselves, in view of their lack of specifity, high toxicity, and associated side effects, not or only to a very restricted extent to therapeutic applications.

Laatsch et al. (Chem. Pharm. Bull. 43(4) 537-546 (1995)) and Fenical (Chem. Rev. 1993, 93, 1673-1683) describe pentabromopseudilin (2,3,4-tribromo-5-(3,5-dibromo-2-hydroxyphenyl)-1H-pyrrole), further pseudilins as well as their anti-tumor and anti-microbial properties.

In view of the limitations of the means and methods of the prior art, the technical problem underlying the present invention was therefore the provision of improved or alternative means and methods for the treatment of myosin-related diseases.

Accordingly, this invention relates to a method of designing a modulator of a myosin, the method comprising molecular modeling of a compound such that the modeled compound interacts with at least three amino acid residues of said myosin, said residues being selected from (a) ranges K265-V268, V411-L441, N588-Q593, D614-T629, and V630-E646 of SEQ ID NO: 2, said myosin comprising or consisting of (i) the sequence of SEQ ID NO: 2; (ii) the sequence encoded by the sequence of SEQ ID NO: 1; (iii) a sequence being at least 40% identical to the sequence of SEQ ID NO: 2 or to the sequence encoded by the sequence of SEQ ID NO: 1; or (iv) a sequence encoded by a sequence being at least 40% identical to the sequence of SEQ ID NO: 1; wherein said sequence of (iii) or (iv) comprises said three amino acid residues, and wherein said residues comprise K265; or (b) ranges of any one of SEQ ID NOs: 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, 80, 82, 84, 86, 88, 90, 92, 94, 96, 98, 100, 102, 104, 106 or 108, respectively, said ranges aligning with the ranges of SEQ ID NO: 2 as defined in (a), said myosin comprising or consisting of (i) the sequence of any one of SEQ ID NO: 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, 80, 82, 84, 86, 88, 90, 92, 94, 96, 98, 100, 102, 104, 106 or 108, respectively; (ii) the sequence encoded by the sequence of any one of SEQ ID NO: 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, 47, 49, 51, 53, 55, 57, 59, 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, 81, 83, 85, 87, 89, 91, 93, 95, 97, 99, 101, 103, 105, 107 or 109, respectively; (iii) a sequence being at least 40% identical to the sequence of any one of SEQ ID NO: 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, 80, 82, 84, 86, 88, 90, 92, 94, 96, 98, 100, 102, 104, 106 or 108, respectively, or to the sequence encoded by the sequence of any one of SEQ ID NO: 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, 47, 49, 51, 53, 55, 57, 59, 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, 81, 83, 85, 87, 89, 91, 93, 95, 97, 99, 101, 103, 105, 107 or 109, respectively; or (iv) a sequence encoded by a sequence being at least 40% identical to the sequence of any one of SEQ ID NO: 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, 47, 49, 51, 53, 55, 57, 59, 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, 81, 83, 85, 87, 89, 91, 93, 95, 97, 99, 101, 103, 105, 107 or 109, respectively; wherein said sequence of (iii) or (iv) comprises said three amino acid residues, and wherein said residues comprise the residue aligning with K265 of SEQ ID. NO: 2; thereby obtaining said modulator of a myosin.

The term “designing” refers to the creation of a molecule, preferably by in silica methods. In addition to in silica methods, further steps may be performed in the method of designing according to the invention, which may include synthesizing of a compound and/or optimization of said compound. Such optional further steps are detailed below.

As regard the in silica methods for creating molecules, these are commonly referred to as molecular modelling. Particularly envisaged for the present invention are molecular modeling tools which are also referred to as ligand construction tools. Such methods for rational drug design typically take into account properties including shape, charge distribution, the distribution of hydrophobic groups, ionic groups and groups capable of forming hydrogen bonds at a site of interests of the protein molecule under consideration. Using this information, that can be derived from the high resolution structure of proteins and protein-ligand complexes (see, e.g. Example 2), these methods either suggest improvements to existing molecules, construct new molecules on their own that are expected to have good binding affinity, screen through virtual compound libraries for such molecules or fragments thereof, or otherwise support interactive design of new drug compounds in silica. Typically, ligand construction makes use of dedicated software and involves interactive sessions in front of a computer display of the three-dimensional structure of the target molecule, i.e., myosin, and of candidate molecules or fragments thereof. Suitable software packages are known in the art and include Chemoffice (CambridgeSoft Corporation), CNS (Acta Cryst. D54, 905-921), CCP4 (Acta Cryst. D50, 760-763), ADF (Computational Chemistry, David Young, Wiley-Interscience, 2001. Appendix A. A.2.1 p. 332) and Gold (G. Jones, P. Willett and R. C. Glen, J. Mol. Biol., 245, 43-53, 1995; G. Jones, P. Willett, R. C. Glen, A. R. Leach and R. Taylor, J. Mol. Biol., 267, 727-748, 1997; M. L Verdonk, J. C. Cole, M. J. Hartshorn, C. W. Murray and R. D. Taylor, Proteins, 52, 609-623, 2003). As a result of modifications of candidate or starting molecules, the modeled compound is obtained.

The coordinates of the target molecule, i.e. myosin, may be experimentally determined e.g. by NMR spectroscopy and/or X-ray crystallography, or may be obtained by molecular modeling, preferably homology modeling using the high resolution structure of a myosin, said high resolution structure being determined by experimental means, to estimate and calculate the structure of a different myosin for which an experimentally determined high resolution structure is not yet available. Suitable software is known in the art and includes the software packages described in Example 2 enclosed herewith. Structures of myosin-2 from Dictyostelium with and without exemplary or preferred compounds are provided in Examples 2 and 7.

The term “interact” or “interaction” as used herein refers to a relation between at least two molecular entities. This relation may inter alia be described in terms of intermolecular distances and/or free energies of interaction. In the first case, an interaction may be defined by at least one intermolecular distance, preferably by more than one such as two, three, four, five or more intermolecular distances. If an interaction according to the invention is to be described in terms of intermolecular distances only, it is envisaged to use at least three such distances. Typically, intermolecular distances are determined as distances between the centers of atoms of the respective interacting molecular entities. In this case, intermolecular distances according to the invention are referred to as interatomic distances. Preferably, a such determined interatomic distance is less than 4 Angstroms, more preferably in the range from 3.6 and 2.8 Angstroms. Preferred values include 3.4, 3.2 and 3.0 Angstroms. Alternatively or in addition, an interaction may be defined in terms of free energy. The free energy may be a total free energy determining the strength of an intermolecular interaction in its entirety or a partial free energy, said partial free energy resulting from, for example, one atom-atom interaction within a plurality of atom-atom interactions within the intermolecular interaction under consideration. Preferably, the total free energy of an interaction according to the invention is at least 60 kJ/mol. This value corresponds to the binding energy of about three hydrogen bonds. More preferred are total free energies of an interaction of at least 100, at least 150 or at least 200 kJ/mol.

As an alternative or additional parameter, and in case of inhibitors, the IC₅₀ concentration may be used to characterize the strength of an intermolecular interaction. The IC₅₀ concentration is the concentration of an inhibitor that is required to inhibit 50% of the target, in the present case myosin. Preferably, the modelled compound, in case it is an inhibitor, interacts with said at least three residues such that the IC₅₀ concentration is in the two-digit micomolar range, i.e. below 100 μM. More preferred are IC₅₀ concentrations below 50 μM, below 10 μM or below 1 μM. Yet more preferred are nanomolar or even picomolar inhibitors, e.g. inhibitors with an IC₅₀ concentration below 100 nM, below 10 nM, below 1 nM or below 100 μM. More generally speaking, and applicable to any binding molecule, the concentration that is required to achieve binding to 50% of the target or modulating of 50% of the target may be used. Preferred values of IC₅₀ concentrations as recited above apply also to these concentrations.

An intermolecular interaction may comprise one or more types of interactions. Types of interactions include charge-charge, charge-dipole, and dipole-dipole interactions and furthermore hydrogen bonds and hydrophobic interactions. Dipoles may be permanent, induced or fluctuating. Interactions involving permanent dipoles and hydrogen bonds may be of particular relevance, since they are capable of specifically positioning and orienting a ligand or modulator in a binding pocket.

The ranges according to part (a) of the main embodiment provide a generic description of the binding pocket according to the present invention. Since at least three residues within these ranges interact with the compound to be modelled, the present invention also provides an implicit definition of pharmacophores capable of binding to said binding pocket. The term “pharmacophore” is known in the art and refers to the molecular framework responsible for the biological or pharmacological activity of a compound (Osman F. Güner (2000) Pharmacophore Perception, Development, and use in Drug Disgn ISBN 0-9636817-6-1; Thierry Langer and Rémy D. Hoffmann (2006) Pharmacophores and Pharmacophore Searches ISBN 3-527-31250-1). Preferred activities of the compound include the modifying of myosin activities as described herein below. Typical pharmacophore features include hydrogen bond donors, hydrogen bond acceptors, dipoles, charges, ions and hydrophobic moieties. The pharmacophore furthermore includes information on the spatial arrangement of one or more of such moieties:

The term “modulator” as used herein refers to any molecule capable of modifying the activity of the target, i.e. myosin. “Modifying” includes increasing and decreasing said activity. The activity includes any molecular, biochemical, biomechanical or biological activity. A preferred activity is the capability of myosin to produce force and/or movement in an actin- and/or Mg-ATP dependent way; see below. A further activity is ATPase activity, i.e., the capability to hydrolyze adenosine trisphosphate (ATP), preferably to yield ADP and P_(i). In structural terms, the modulator is not limited. Preferably, the modulator is a small organic molecule, the term “small” preferably referring to molecules with a molecular weight below 1200, 1000, 800, 600, 500, 400 or 300 Da.

The term “myosin” refers to a well-known class of proteins with ATPase activity and having the capability of generating force and/or directional movement; see also the background section herein above. Table 1 below provides further information on myosins to be used in the present invention.

1: Summary of Myosins NCBI Accession Class Subclass Myosin (name) number Function Literature 1 BBM Hs Moysin-1A (MYO1A) NM_005379; Cell motility Bement et al., 1994, Iα Hs Myosin-1B (MYO1B) AF127026; Vesicular transport Hofmann et al., 2006 Iβ Hs Myosin-1C (MYO1C) AF009961 Endocytosis Ruppert et al., 1993, 1γ Hs Myosin-1D (MYO1D) NM_012223; Exocytosis Salas-Cortes et al., 2005 IC Hs Myosin-1E (MYO1E) XM_290989 Signal transduction Bement et al., 1994; - — Hs Myosin-1F (MYO1F) NM_001080779 Transcription Hasson et al., 1996; - — Hs Myosin-1G (MYO1G) NM_015194; Trafficking Bement et al., 1994; — Hs Myosin-1H (MYO1H) XM_050041 Neurosensory functions Krendel et al., 2007 NM_004998 Cell morphology Crozet et al., 1997; - NM_012335 Left-right asymmetry Scherer et al., 2003; - NM_033054; Venter et al., 2001; - XM_291223, XM_374431 NM_001101421; XM_001125815 2 Skeletal muscle Hs heavy chain 1 (MYH1), skeletal muscle NM_005963 Muscle contraction Leinwand et al., 1983 Cardiac muscle (adult) NM_017534 Muscle contraction Eller, et al., 1989 non-muscle Hs heavy chain 2 (MYH2), skeletal muscle NM_001100112 Cytokinesis, cortical Winters et al., 1998; smooth muscle (adult, var1) NM_002470 bundling, morphogenesis, Schachat and Briggs, 2002 Extra ocular Hs heavy chain 2 (MYH2), skeletal muscle NM_017533 cell motility/migration, Solomon et al., 1990 Not defined (adult, var2) NM_003802 carcinogenesis Solomon et al., 1990; Not defined Hs heavy chain 3 (MYH3), skeletal muscle NM_002471 Muscle contraction Pegoraro et al., 2007 Not defined (embryonic) NM_000257 Desjardins et al., 2002 Hs heavy chain 4 (MYH4), skeletal muscle XM_371398 Simons et al., 1991 Hs heavy chain 13 (MYH13), skeletal muscle NM_002473 Andzelm et al., 2007 Hs heavy chain 8 (MYH8), skeletal perinatal XM_290747 Matsuoka et al., 1993; Hs heavy chain 6 (MYH6), cardiac muscle NM_002474; Zhang et al., 2006 alpha NM_022870 Desjardins et al., 2002 Hs heavy chain 7 (MYH7), cardiac muscle beta NM_001040114 Desjardins et al., 2002; Hs heavy chain 7 (MYH7B), cardiac muscle NM_022844 Donaudy et al., 2004 beta NM_001040113 Desjardins et al., 2002 Hs heavy chain 9 (MYH9), non muscle NM_001077186 Hs heavy chain 10 (MYH10), non-muscle NM_024729 Hs heavy chain 11 (MYH11), smooth muscle NM_014981; varSM1A XM_036988; Hs heavy chain 11 (MYH11), smooth muscle XM_938225 varSM1B Hs heavy chain 11 (MYH11), smooth muscle varSM2A Hs heavy chain 11 (MYH11), smooth muscle varSM2B Hs heavy chain 13 (MYH13) Hs heavy chain 14 (MYH14), var1 Hs heavy chain 14 (MYH14), var2 Hs heavy chain 15 (MYH15) 3 Myosin-3a Hs myosin-3A (Myo3A) NM_017433 Phototransduction and Dose et al., 2000; Myosin-3b Hs myosin-3B (Myo3B), var1 NM_001083615 hearing processes Walsh et al., 2002 Dose and Burnside, 2002 5 Myosin-5a Hs Myosin-5a (MYO5A) NM_00259 Intracellular trafficking Engle and Kennett, 1994; Myosin-5b Hs Myosin-5b (MYO5B) NM_001080467; and transport processes Desnos et al., 2007 Myosin-5c Hs Myosin-5c (MYO5C) XM_371116 (mitochondrial transport, Bement et al., 1994; NM_018728 melanosomal transport, Lapierre et al., 2001 mRNA, organelles, cargo) Bement et al., 1994; in neuronal cells and other Rodriguez and Cheney, 2002 cell types 6 Myosin-6 Hs myosin-6 (MYO6) NM_004999; Reverese directional Bement et al., 1994; XM376516 transport processes, Dunn et al., 2006 clathrin-mediated endocytosis, neurosensory functions 7 Myosin-7a Hs myosin-7a (MYO7A) NM_000260 Cell adhesion, filopodia Bement et al., 1994; extensions, stereocilia Jaijo et al., 2007 organization, neurosensory functions 9 Myosin-9a Hs myosin-9a (MYO9A) NM_006901 Signaltransduction Bement et al., 1994 Myosin-9b Hs myosin-9b (MYO9B) NM_004145 Lamellipodia, fillopodia Bement et al., 1994; extensions Sanchez et al., 2007 10 Myosin-10 Hs myosin 10 (MYO10) NM_012334 Filopodia Hasson et al., 1996; formation/dynamics Bohil et al., 2006 Function in cell motility Neuronal growth cone 11 Myosin-11 Plant myosins (tobacco, Arabidopsis Cytoplasmic streaming Shimmen, 2007; thaliana, . . .) Transport Lee and Liu, 2004; Volkmann et al., 2003 14 Toxoplasma Tg myosin-A (TgMyoA) AF006626 Gliding motility host cell Heintzelman and gondii Tg myosin-B (TgMyoB) AF438184 invasion processes Schwartzman, 1997 Plasmodium Tg myosin-E (TgMyoE) AF221131 Delbao et al., 2001 falciparum Pf myosin-A AF105117 Delbao and Soldati, unpublished Foth et al., 2006 15 Myosin-15a Hs unconventional myosin-15a (Myo15A) AF144094 Neurosensory functions Liang et al., 1999 Myosin-15b Hs unconventional myosin-15b (Myo15B) NR_003587 Berg et al., 2001; Boger et al., 2001 16 Myosin-16 Hs myosin-16 (Myo16) BC146791 Neuronal functions Strausberg et al., 2002 18 Myosin-18a Hs myosin-18a (MYO18A), var1 NM_078471 “Carcinogenesis” Furusawa et al., 2000; Myosin-18b Hs myosin-18a (MYO18A), var2 NM_203318 Mori et al., 2003 Hs myosin-18b (MYO18B) NM_032608 Mori et al, 2003; Yang et al., 2005 Dunham et al., 1999; Edakuni et al., 2006 19 Myosin-19 Hs myosin-19 (Myo19) BC008900 ? Strausberg et al., 2002 22 Toxoplasma Tgmyosin-F (TgMyoF) DQ131541 Invasion processes, . . . Foth et al., 2006 gondii

Sequence alignments of myosins motor domains are shown in the Figures enclosed herewith. These sequence alignments have been created with methods well known and established in the art. The multiple sequence alignments have been generated with the software ClustalW (see below) by using the following parameters: Gap Penalty: 15.00; Gap Length Penalty: 0.5; Delay Divergent Seqs (%): 15; Protein Weight Matrix: Gonnet Series.

The invention is applicable to all myosin isoforms, in particular to the myosins having sequences of the sequence listing. Several sequences of the sequence listing correspond to sequences with the below accession numbers for the NCBI databases (www.pubmed.com) in the versions of Nov. 11, 2008. Preferred myosin isoforms are human, Apicomplexa and plant isoforms.

Human Myosins

-   -   1. H.s. myosin IA (MYO1A), NM_(—)005379     -   2. H.s. myosin IB (MYO1B), NM_(—)012223     -   3. H.s. myosin IC (MYO1C), NM_(—)001080779     -   4. H.s. myosin ID (MYO1D), NM_(—)015194     -   5. H.s. myosin IE (MYO1E), NM_(—)004998     -   6. H.s. myosin IF (MYO1F), NM_(—)012335     -   7. H.s. myosin IG (MYO1G), NM_(—)033054     -   8. H.s. myosin IH (MYO1H), NM_(—)1001101421     -   9. H.s. myosin heavy chain 1, skeletal muscle, adult (MYH1),         NM_(—)005963     -   10. H.s. myosin heavy chain 2, skeletal muscle, adult (MYH2),         NM_(—)017534     -   11. H.s. myosin heavy chain 3, skeletal muscle, embryonic,         (MYH3), NM_(—)002470     -   12. H.s. myosin heavy chain 4, skeletal muscle (MYH4),         NM_(—)017533     -   13. H.s. myosin heavy chain 6, cardiac muscle alpha (MYH6),         NM_(—)002471     -   14. H.s. myosin heavy chain 7, cardiac muscle, beta (MYH7),         NM_(—)000257     -   15. H.s. myosin heavy chain 7B, cardiac muscle, beta (MYH7B),         NM_(—)020884     -   16. H.s. myosin heavy chain 8, skeletal muscle perinatal (MYH8),         NM_(—)002472     -   17. H.s. myosin heavy chain 9, non-muscle (MYH9), NM_(—)002473     -   18. H.s. myosin heavy chain 10, non-muscle (MYH10), NM_(—)005964     -   19. myosin heavy chain 11, smooth muscle A (MYH11),         NM_(—)002474; NM_(—)022844     -   20. H.s. myosin heavy chain 11, smooth muscle B (MYH11),         NM_(—)001040114; NM_(—)001040113     -   21. H.s. myosin heavy chain 13, skeletal muscle (MYH13),         NM_(—)003802     -   22. H.s. myosin heavy chain 14 (MYH14), AY 165122     -   23. H.s. myosin heavy chain 14 (MYH14), NM_(—)001077186,         NM_(—)024729     -   24. H.s. myosin heavy chain 15 (MYH15), NM_(—)014981     -   25. H.s. myosin IIIA (MYO3A), NM_(—)017433     -   26. H.s. myosin IIIB (MYO3B), NM_(—)001083615     -   27. H.s. myosin VA (MYO5A), NM_(—)000259     -   28. H.s. myosin VB (MYO5B), NM_(—)001080467     -   29. H.s. myosin VC (MYO5C), NP_(—)061198     -   30. H.s. myosin VI (MYO6), NM_(—)004999     -   31. H.s. myosin VIIA (MYO7A), NM_(—)000260     -   32. H.s. myosin IXA (MYO9A), NM_(—)006901     -   33. H.s. myosin IXB (MYO9B), NM_(—)004145     -   34. H.s. myosin X (MYO10), NM_(—)012334     -   35. H.s. myosin XVA (MYO15A), AF144094     -   36. H.s. myosin XVI (MYO16, Myr8), NP_(—)055826     -   37. H.s. myosin XVIIIA (MYO18A), NM_(—)078471; NM_(—)203318     -   38. H.s. myosin XVIIIB (MYO18B), NM_(—)032608     -   39. H.s. myosin XIX (MYO19), BC008900

Plasmodium and Toxoplasma Myosins

-   -   1. P.f. MyoA, AF105117     -   2. P.f. MyoF, Q286V9     -   3. T.g. MyoA, AF006626     -   4. T.g. MyoB, AF438184     -   5. T.g. MyoC, AF438183     -   6. T.g. MyoD, AF105118     -   7. T.g. MyoF, DQ131541

The ranges as defined in part (b) of the main embodiment are readily determined based on (i) the information regarding the ranges in the sequence of SEQ ID NO: 2 (myosin-2) as defined in part (a) of the main embodiment and (ii) said sequence alignments. Preferably, the alignment of said ranges occurs over the entire length of the respective ranges as recited in parts (a) and (b); see also the enclosed alignments (in particular FIGS. 2 to 4).

For example, the corresponding, i.e., aligning ranges in the sequence of SEQ ID NO: 4 (myosin-1) are as follows: K186-V190, C342-N362, N523-F528, P549-T561, and A562-L577, and the corresponding ranges in the sequence of SEQ ID NO: 6 (myosin-5) are as follows: K246-V250, K392-N413, N568-Y573, L613-T635, and V636-L651.

These ranges as well as the ranges recited in part (a) of the main embodiment define structural elements of the three-dimensional structure of the respective myosin or secondary structure elements thereof. In particular, the five ranges in their respective order correspond to the following structural elements, the designations of which are established in the art: helix 13, helix 21, strut loop, loop2, and helix-29; see also the enclosed multiple sequence alignments (in particular FIGS. 2 to 4) as well as the schematic drawing of the topology of myosin-2 (FIG. 1). As shown in the enclosed Figures, these structural elements form a previously unknown binding pocket of myosins. This binding pocket was found by the present inventors to be an allosteric binding pocket. The term “allosteric” is known in the art and refers to an alteration of conformation in response to ligand binding. Ligand binding occurs at a site which is not the active site or one of the active sites of the target (here myosin), but exerts a modulating effect on the active site(s). This modulation involves structural changes which in turn frequently entail functional changes. In other words, binding of ligands to this pocket induces or locks, respectively, a conformation of myosin. The induced or locked conformation may be an active or inactive conformation. The term “activity” is defined herein above. Preferably, said induced or locked conformation is an inactive conformation, e.g. a conformation of myosin with reduced or absent ATPase activity and/or reduced or absent actin binding capability and/or force generating activity. Alternatively, said induced or locked conformation may be an activated conformation. It is preferred that the activated conformation has a higher force generating activity.

The amino acid residues K265 as recited in part (a) is an anchor residue for the interaction of a modulator with the binding pocket defined by the ranges recited in part (a). A corresponding anchor residue in the sequence of SEQ ID NO: 4 (myosin-1) is K186. A corresponding anchor residue in the sequence of SEQ ID NO: 6 (myosin-5) is K246. Corresponding anchor residues of further myosins can be determined from the enclosed multiple sequence alignments without further ado. As used herein, the term “anchor residue” refers to residues of particular relevance for the interaction between a myosin and a modulator thereof. The residue of any myosin which aligns with K265 of SEQ ID NO: 2 (myosin-2) is almost invariably a Lys residue. It may also be an Arg residue.

Sequence identity levels as recited in the main embodiment may be determined by methods well known in the art. Two nucleotide or protein sequences can be aligned electronically using suitable computer programs known in the art. Such programs comprise BLAST (Altschul et al. (1990), J. Mol. Biol. 215, 403-410), variants thereof such as WU-BLAST (Altschul & Gish (1996), Methods Enzymol. 266, 460-480), FASTA (Pearson & Lipman (1988), Proc. Natl. Acad. Sci. USA 85, 2444-2448), CLUSTALW (Higgins et al. (1994), Nucleic Acids Res. 22, 4673-4680) or implementations of the Smith-Waterman algorithm (SSEARCH, Smith & Waterman (1981), J. Mol. Biol. 147, 195-197). These programs, in addition to providing a pairwise sequence alignment (multiple sequence alignment in case of CLUSTALW), also report the sequence identity level (usually in percent identity) and the probability for the occurrence of the alignment by chance (P-value).

Preferably the sequence identity at the amino acid sequence level between myosins is at least 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98% or 99%. Preferred sequence identities at the nucleic acid sequence level are at least 50%, 60%, 70%, 75%, 80%, 85%, 90%, 92%, 94%, 95%, 96%, 97%, 98% or 99%. In any case, it is deliberately envisaged to use myosins from mammalian and avian species including Rattus norvegicus, Mus musculus, Gallus gallus, Lepus europaeus and Canis lupus.

In a further embodiment, the method of designing of the invention further comprises synthesizing said modulator, thereby producing said modulator. The subject-matter of this embodiment is a method of producing said modulator. This embodiment is particularly envisaged for those cases where the modulator is a small organic molecule, a peptide or protein. Means and methods for synthesizing peptides and proteins are well known in the art and may involve organic synthesis and/or the recombinant production using the methods of molecular biology and protein biochemistry. As regards small organic molecules, reference is made to the Beilstein database available from MDL Information Systems as an example. Means and methods for preparing the preferred compound classes (for details see below) to be used in screens according to the invention are detailed in the Examples enclosed herewith. In a further preferred embodiment, said molecular modeling comprises (i) measuring at least one intermolecular distance; (ii) calculating at least one free energy of interaction; and/or (iii) determining the accessibility to the allosteric binding pocket. Accessibility of the binding pocket limits the size of the allosteric effector and thereby the maximal intermolecular interaction energy.

Tools for molecular modeling as described above typically provide the option of measuring one or more intermolecular distances. Preferably, the intermolecular distances are determined as distances between the centers of atoms. Tools for molecular modeling also generally provide the option of calculating free energies of interaction. The term “free energy” in relation to an interaction is well known in the art and is related to the equilibrium binding constant by the equation ΔG=−RT ln K, wherein ΔG is the change in free energy upon binding, K is the binding constant, T is the temperature and R is the universal gas constant. Free energies to be calculated may be, as described above, total free energies and/or partial free energies.

In a further preferred embodiment, said ranges as defined in part (a) of the main embodiment are limited to the following positions: K265, A420, K423, A424, R428, L431, D590, I617, and A618. These positions or at least three of these positions provide a preferred definition of the binding pocket according to the invention. By defining the binding pocket, they implicitly also define the pharmacophore which is capable of binding to said binding pocket.

In case of the sequence of SEQ ID NO: 4 (myosin-1), preferred positions are K186, A355, E358, R359 N362, D521 and L527. Said preferred positions are located within the ranges as defined in the main embodiment. In case of the sequence of SEQ ID NO: 6 (myosin-5), preferred positions are K246, A402, H406, A409, N410, N413, D570, V572 and H632. Obviously, in further preferred embodiments of part (b) of the main embodiment (said preferred embodiments relating to SEQ ID NOs: 8 to 108 (even numbers)), preferred positions are those positions which align with K265, A420, K423, A424, R428, L431, D590, I617, and A618 of SEQ ID NO: 2. Analogous considerations apply to all preferred positions or ranges.

Further preferred anchor residues for modulator binding (in addition to the Lys residue described above) include D590 in the strut loop in Dictyostelium myosin-2 (SEQ ID NO: 2), which corresponds to D521 in Dictyostelium myosin-1 (SEQ ID NO: 4) and to D570 in Gallus gallus myosin-5 (SEQ ID NO: 6), respectively.

On the other hand, there residues in the allosteric binding pocket according to the invention which are specific for a given subclass of myosins such as class 2 myosins. Preferably, the method of designing according to the invention makes use of such subclass-specific residues to the effect that said modeled compound interacts with at least one of said subclass-specific residues. Modeled compounds interacting with at least one of said subclass-specific residues are candidates for subclass-specific modulators. More specifically, specificity is mostly mediated by residues in helix-21 that connects the actin binding cardiomyopathy loop (formed by residues 403 to 406 in myosin 2 (SEQ ID NO: 2)) with strand β5 which is part of the central β-sheet and adjacent to switch-2, forming part of the nucleotide binding pocket. The multiple contacts in helix-21 are structurally conserved but diverse as regards the nature of side chains involved in interactions. Conserved residues are A424, R428, and L431 in myosin-2 (SEQ ID NO: 2), A355, R359, and N362 in myosin-1 (SEQ ID NO: 4), and H406, N410, N413 in myosin-5 (SEQ ID NO: 6), respectively. Additional, preferably subclass-specific contacts with a compound binding to the allosteric pocket are provided by residues belonging to loop-2 and helix-29. The latter contacts are neither structurally conserved nor at the level of the side chains and thereby provide further possibilities in fine-tuning inhibitor binding and subclass-specificity thereof. Residues belonging to loop-2 and helix-29 are of particular importance in forming the opening of the access channel to the allosteric binding site of the invention. Specific residues in this region can be selected from the annotated sequence alignments and the topology diagram enclosed herewith (FIGS. 1 to 4).

The present invention furthermore provides a method of identifying a modulator of a myosin, the method comprising (a) bringing into contact a myosin and a test compound; (b) determining whether said test compound interacts with at least three amino acid residues selected from (ba) ranges K265-V268, V411-L441, N588-Q593, D614-T629, and V630-E646 of SEQ ID NO: 2, said myosin comprising or consisting of (i) the sequence of SEQ ID NO: 2; (ii) the sequence encoded by the sequence of SEQ ID NO: 1; (iii) a sequence being at least 40% identical to the sequence of SEQ ID NO: 2 or to the sequence encoded by the sequence of SEQ ID NO: 1; or (iv) a sequence encoded by a sequence being at least 40% identical to the sequence of SEQ ID NO: 1; wherein said sequence of (iii) or (iv) comprises said three amino, acid residues, and wherein said residues comprise K265; or (bb) ranges of any one of SEQ ID NOs: 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, 80, 82, 84, 86, 88, 90, 92, 94, 96, 98, 100, 102, 104, 106 or 108, respectively, said ranges aligning with the ranges of SEQ ID NO: 2 as defined in (a), said myosin comprising or consisting of (i) the sequence of any one of SEQ ID NO: 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, 80, 82, 84, 86, 88, 90, 92, 94, 96, 98, 100, 102, 104, 106 or 108, respectively; (ii) the sequence encoded by the sequence of any one of SEQ ID NO: 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, 47, 49, 51, 53, 55, 57, 59, 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, 81, 83, 85, 87, 89, 91, 93, 95, 97, 99, 101, 103, 105, 107 or 109, respectively; (iii) a sequence being at least 40% identical to the sequence of any one of SEQ ID NO: 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, 80, 82, 84, 86, 88, 90, 92, 94, 96, 98, 100, 102, 104, 106 or 108, respectively, or to the sequence encoded by the sequence of any one of SEQ ID NO: 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, 47, 49, 51, 53, 55, 57, 59, 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, 81, 83, 85, 87, 89, 91, 93, 95, 97, 99, 101, 103, 105, 107 or 109, respectively; or (iv) a sequence encoded by a sequence being at least 40% identical to the sequence of any one of SEQ ID NO: 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, 47, 49, 51, 53, 55, 57, 59, 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, 81, 83, 85, 87, 89, 91, 93, 95, 97, 99, 101, 103, 105, 107 or 109, respectively; wherein said sequence of (iii) or (iv) comprises said three amino acid residues, and wherein said residues comprise the residue aligning with K265 of SEQ ID NO: 2; and (c) identifying those compounds which interact with said at least three amino acid residues, thereby indentifying said modulator of a myosin.

This embodiment relates to a screen for the identification of myosin modulators which in turn are suitable as medicaments or lead compounds for the development of a medicament. The screen may be implemented in various ways such as a biochemical screen or a cellular screen. In case of a cellular screen said “bringing into contact a myosin and a test compound” may be effected by bringing into contact a cell producing a myosin with a test compound. The bringing into contact is performed under conditions which allow binding of the test compound to myosin, in case the test compound is in principle capable of binding. Suitable conditions include conditions in liquid phase such as aqueous solutions, preferably buffered solutions. Furthermore, ionic strength may be adjusted, e.g., by the addition of sodium chloride. The concentration of sodium chloride may be between 0 and 2 M, preferably between 100 and 200 mM. Alternatively, sodium chloride is absent from the assay. For biological assays in many cases the presence of one or more further substances, including other salts than sodium chloride, trace elements, anti-oxidants, amino acids, vitamins, growth factors, ubiquitous co-factors such as ATP or GTP, is required. Said further substances may either be added individually or provided in complex mixtures such as serum. These and further accessory substances are well known in the art as are concentrations suitable for biological assays. The skilled person is aware of suitable conditions in dependency of the particular assay format to be used in the method of screening according to the invention.

In a further embodiment, the screen may be implemented as a virtual screen, i.e., the screen may be performed in silico. Virtual screens may be implemented by computer-based docking of one test compound at a time into the allosteric binding site defined above, wherein both the test compound and the binding site are represented in silico. Thereby, the binding position and conformation is calculated. The binding site may, for example, be comprised in a representation of the entire myosin molecule or, alternatively, of those parts only which line the binding pocket. Upon completion of docking, the binding affinity (or equivalently the free energy of interaction as defined herein above) is determined based on the parameters of the computer representation of the involved molecules. A threshold may be chosen such as to select those test compounds which are candidate high affinity binders. Suitable software packages are known in the art and include Chemoffice, CNS, CCP4, ADF and Gold (see above).

Preferably, said determining in step (b) is effected by X-ray crystallography and/or NMR spectroscopy.

In other words, the question of whether an interaction involving at least three residues of myosin occurs, is answered by determining structural parameters by using NMR spectroscopy or X-ray crystallography. These structural parameters may comprise the coordinates of the complex between said test compound and myosin. Alternatively, structural parameters may be determined only to the extent necessary to determine whether binding according to the invention, in particular interaction with at least three residues of myosin occurs. Examples of the latter, more selective methods include NMR spectroscopic methods exploiting the nuclear Overhauser effect or saturation transfer difference (STD). Suitable methods include the recording of NOESY and/or ROESY spectra. The required NMR spectra can be obtained in medium to high throughput manner, wherein throughput may be further increased by assessing a mixture of ligands, for example 10, 20 or 100 ligands at a time and further analyzing only those mixtures which are found to comprise one or more binding molecules. Also, means and methods for high throughput crystallization are available; see, for example, Stevens (Current Opinion in Structural Biology 2000, 10: 558-564) and Kuhn et al. (Current Opinion in Chemical Biology 2002, 6: 704-710).

In a preferred embodiment, X-ray crystallography comprises (a) generating a crystal of a complex formed by said test compound bound to myosin; (b) generating and recording x-ray diffraction data; (c) digitising the data; (d) calculating an electron density map; (e) determining the three-dimensional structure of the crystal components; and (f) storing the crystal coordinates generated on a data carrier.

X-ray diffraction may be performed on a beamline such as the 1029 beamline of ESRF, Grenoble or using in-house devices such as a Bruker X8PROTEUM. Data may be further processed with XDS (W. Kabsch, J. Appl. Cryst. 21, 67 (1988)) and refined with CNS (A. T. Brünger et al. Acta Cryst. D 54, 905 (1998)). Alternatively, the PROTEUM2 software (Bruker) may be used. Structure can finally be solved with, for example, AmoRe (J. Navaza, Acta Crystallogr. A 50, 157 (1994)) and analysed with Xfit (D. E. McRee, J. Struct. Biol. 125, 156 (1999)) while structure validatation may be performed with PROCHECK (R. A. Laskowski, M. W. MacArthur, J. Appl. Crystallogr. 26, 283 (1993)) and WHATCHECK (R. W. W. Hoot G. Vriend, C. Sander, E. E. Abola, Nature 381, 272 (1996)). The final map containing the atomic coordinates of the constituents of the crystal may be stored on a data carrier, typically the data is stored in PDB format or in X_PLOR format, both of which are known to the person skilled in the art. However, crystal coordinates may as well be stored in simple tables or text files.

In a preferred embodiment, the myosin used in the screen involving X-ray crystallography according to the invention is myosin-2. A co-crystal of myosin-2 with an exemplary inhibitor has been solved; see Example 2. Methods well know in the art such as soaking permit the generation of co-crystals of myosin-2 with other modulators. Performing X-ray crystallography according to the invention with such co-crystals is a means of providing the necessary information for identifying compounds which interact with said at least three amino acid residues.

In a preferred embodiment of the method of identifying according to the invention, said method further comprises the step of (a′) (i) determining whether said test compound binds to said myosin; and/or (ii) determining whether said test compound modulates the activity and/or conformation of said myosin; and/or (iii) determining the cytotoxicity of said test compound; wherein step (a) is to be effected after step (a) and prior to step (b), and wherein said determining in step (b) is performed with test compounds determined to bind, to modulate, and/or to be cytotoxic in step (a′).

This embodiment provides for filtering a subset of test compounds testing positive in one or more of the assays of (a′) (i) to (iii). The advantage of such filtering is that the subsequent determining whether the test compound interacts with at least three residues has to be done only with said test compounds testing positive.

Means and methods for determining binding are well known in the art and include assays based on fluorescence such as fluorescence resonance energy transfer (FRET) assays and fluorescence polarization (FP) assays, immunological assays such as ELISA, surface plasmon resonance, isothermal titration calorimetry and Fourier Transformed Infrared Spectroscopy (FTIR).

Assays for myosin activity are discussed further below.

Since the method of identifying a modulator according to the invention is designed to identify compounds binding to the allosteric pocket of myosins, an additional or alternative filtering step involves the determining whether the test compound modulates or changes the conformation of said myosin. A change in conformation may be determined by using methods known in the art including the determination of electrophoretic or chromatographic mobility and fluorescence-based methods. In the latter case, changes in intramolecular distances between fluorophors arising from a change of conformation may be determined.

Said cytotoxicity correlates with the inhibition of the ATPase activity of myosin. Cytotoxicity may be assayed by determining the cellular uptake of neutral red. Only living cells are capable of neutral red uptake via an active transport mechanism. For an exemplary workflow of a cytotoxicity assay, see FIG. 16.

Preferably, said activity is the capability of said myosin (i) to bind actin; (ii) to convert ATP into ADP and P_(i); and/or (iii) to generate force and/or movement. Exemplary or preferred binding assays are described herein above and can be applied for determining whether myosin binds actin, preferably F-actin, and/or nucleotides. Exemplary or preferred activity assays are described herein below and can be applied for determining whether myosin is capable of converting ATP into ADP and P_(i) or of force production and generation of movement. An exemplary assay for ATPase activity is based on the detection of free phosphate formed upon cleavage of ATP, wherein the detection is effected using malachite green. For an exemplary workflow, see FIG. 17.

In preferred embodiments, molecular modeling according to the invention starts from a compound selected from compounds of the general formulae (1) to (4) or a salt or solvate thereof, or the test compound to be used in methods of identifying of the invention is selected from compounds of the general formulae (1) to (4) or a salt or solvate thereof

wherein X is selected from NH, O and S; and Y and Z designate, as valence permits, one or more substituents, wherein each occurrence of Y and Z is independently selected from F, Cl, Br, I, R and OR; R being selected from (i) H, (ii) (CO)CH₃, and (iii) linear or branched alkyl, alkenyl or alkinyl with one to four carbon atoms, the moieties (ii) and (iii) being optionally substituted with one or more F, Cl, Br and/or I.

Formula (1) represents carbazoles, dibenzofurans and dibenzothiophenes according to the invention. Formula (2) represents acridones according to the invention. Formula (3) represents a group of alkaloids known as pseudilines as well as their structural analogues having furan or thiophene in place of the pyrrole ring. Formula (4) represents quinolines according to the invention. The nitrogen-containing ring of quinolines according to the invention may be partially or fully hydrogenated.

Generally, in preferred embodiments of the present invention, R—as used in conjunction with any of the general formulae disclosed herein above and below—has one or two carbon atoms. Particularly preferred is R=CH₃, CCl₃ or CF₃. Also preferred are partially halogenated or mixed halogenated methyl groups such as CH₂F, CHF₂, CH₂Cl, CHCl₂, CF₂Cl or CHFCl.

Further preferred compounds are disclosed herein below in conjunction with medical uses. All compounds described in conjunction with medical uses, in particular classes of compounds represented by generic formulae, are deliberately envisaged for use in the methods according to the present invention.

Also provided is the use of a compound selected from compounds of the general formulae (1) to (4) or a salt or solvate thereof as a lead compound in the development of a modulator of a myosin.

The term “lead compound” is known in the art and refers to a compound providing a starting point for developing a pharmaceutically active agent. Generally, said pharmaceutically active agent is different from, preferably optimized as compared to the lead compound. In other words, the development of a lead compound preferably involves the optimization of the pharmacological properties of said lead compound.

Methods for the optimization of the pharmacological properties of compounds identified in screens, generally referred to as lead compounds, are known in the art and comprise a method of modifying a compound identified as a lead compound to achieve: (i) modified site of action, spectrum of activity, organ specificity, and/or (ii) improved potency, and/or (iii) decreased toxicity (improved therapeutic index), and/or (iv) decreased side effects, and/or (v) modified onset of therapeutic action, duration of effect, and/or (vi) modified pharmacokinetic parameters (resorption, distribution, metabolism and excretion), and/or (vii) modified physico-chemical parameters (solubility, hygroscopicity, color, taste, odor, stability, state), and/or (viii) improved general specificity, organ/tissue specificity, and/or (ix) optimized application form and route by (i) esterification of carboxyl groups, or (ii) esterification of hydroxyl groups with carboxylic acids, or (iii) esterification of hydroxyl groups to, e.g. phosphates, pyrophosphates or sulfates or hemi-succinates, or (iv) formation of pharmaceutically acceptable salts, or (v) formation of pharmaceutically acceptable complexes, or (vi) synthesis of pharmacologically active polymers, or (vii) introduction of hydrophilic moieties, or (viii) introduction/exchange of substituents on aromates or side chains, change of substituent pattern, or (ix) modification by introduction of isosteric or bioisosteric moieties, or (x) synthesis of homologous compounds, or (xi) introduction of branched side chains, or (xii) conversion of alkyl substituents to cyclic analogues, or (xiii) derivatisation of hydroxyl group to ketales, acetales, or (xiv) N-acetylation to amides, phenylcarbamates, or (xv) synthesis of Mannich bases, imines, or (xvi) transformation of ketones or aldehydes to Schiff's bases, oximes, acetates, ketales, enolesters, oxazolidines, thiazolidines or combinations thereof.

The various steps recited above are generally known in the art. They include or rely on quantitative structure-action relationship (QSAR) analyses (Kubinyi, “Hausch-Analysis and Related Approaches”, VCH Verlag, Weinheim, 1992), combinatorial biochemistry, classical chemistry and others (see, for example, Holzgrabe and Bechtold, Deutsche Apotheker Zeitung 140(8), 813-823, 2000).

Preferably, said general formulae are the general formulae (1) or (2).

In a further preferred embodiment, said modulator is an inhibitor.

The term “inhibitor” refers to compounds lowering or abolishing the activity of myosin, whereas the term “activator” refers to compounds increasing the activity of myosin, said activity being defined herein above. In preferred embodiments, inhibition refers to a reduction in activity of at least 10, 20, 30, 40, 50, 60, 70, 80, 90, 95, 98 or 99%. More preferred, activity drops to less than 10⁻², less than 10⁻³, less than 10⁻⁴ or less than 10⁻⁵ times the activity in absence of the inhibitor. “Activation” preferably refers to an increase in activity by 10, 20, 50 or 100%. More preferred activation involves a rise in activity to 3-fold, 5-fold, 10-fold or 15-fold or more of the activity in absence of the activator.

The present invention furthermore provides a pharmaceutical composition comprising one or more compounds selected from compounds of the general formulae (1), (2) and (4) as defined herein above; 2,3,4-tribromo-5-(1′-methoxy-2′,4′-difluoro-phenyl)-pyrrole; and the compounds shown below, wherein CF₃ may replace one, more or all occurrences of F, Cl, Br and/or MeO in said compounds shown below:

or a salt or solvate thereof.

The pharmaceutical composition may further comprise pharmaceutically acceptable carriers, excipients and/or diluents. Examples of suitable pharmaceutical carriers, excipients and/or diluents are well known in the art and include phosphate buffered saline solutions, water, emulsions, such as oil/water emulsions, various types of wetting agents, sterile solutions etc. Compositions comprising such carriers can be formulated by well known conventional methods. These pharmaceutical compositions can be administered to the subject at a suitable dose. Administration of the suitable compositions may be effected by different ways, e.g., by intravenous, intraperitoneal, subcutaneous, intramuscular, topical, intradermal, intranasal or intrabronchial administration. It is particularly preferred that said administration is carried out by injection and/or delivery, e.g., to a site in the pancreas or into a brain artery or directly into brain tissue. The compositions may also be administered directly to the target site, e.g., by biolistic delivery to an external or internal target site, like the pancreas or brain. The dosage regimen will be determined by the attending physician and clinical factors. As is well known in the medical arts, dosages for any one patient depends upon many factors, including the patient's size, body surface area, age, the particular compound to be administered, sex, time and route of administration, general health, and other drugs being administered concurrently. Pharmaceutically active matter may be present in amounts between 1 ng and 10 mg/kg body weight per dose; however, doses below or above this exemplary range are envisioned, especially considering the aforementioned factors. If the regimen is a continuous infusion, it is preferably in the range of 1 μg to 10 mg units per kilogram of body weight per minute.

Also provided is the use of one or more compounds as defined above for the manufacture a pharmaceutical composition for the treatment and/or prevention of cardiovascular diseases, cancer, diseases of the central nervous system, viral infections, and infections by parasites of the Apicomplexa family.

Example 2 provides proof of in vitro and in vivo activity of several preferred or exemplary compounds of the invention.

Myosins play an essential role in force generating processes and are essential in several common diseases like cancer, cardiovascular diseases, and parasite and viral infections. Also the immune response during inflammation, which is triggered by the synapse between T cells and antigen presenting cells, depends on the activation of myosin-2 and myosin-5 and is up-regulated during T-cell activation (Rey et al., 2007, in press).

With respect to cancer, in particular the formation of metastasis severely complicates the therapy and negatively affects the prognosis. At the beginning of tumor metastasis cells may enter into an amoeboid migratory state. For the migration, non-muscle myosins-2A and 2B play an essential role (Betapudi et al., 2006). The inhibition of myosin-2 (in particular isoform A) was shown to strongly inhibit tumor cell migration. Furthermore, in a clinical study on lung cancer patients a positive correlation was found between the expression of a myosin acitivating enzyme (myosin light chain kinase) and the likelihood of disease recurrence and metastasis (Minamiya et al., 2005). These and additional observations give strong evidence that the myosin-2 isoforms are excellent target proteins for cancer treatment, in particular against tumors that may form metastasis. This holds true in particular for the prevalent cancer types with high incidence (U.S. cancer statistics from 2003) like cancer of the oral cavity and pharynx, the digestive system including pancreas and respiratory system, melanomas of the skin, the genital and urinary system, and cancer of the brain and the nervous system. Further cancer forms which are deliberately envisaged for treatment by the present invention are listed below.

The myosin isoform 2B was found to be important for lamellar protrusions of migrating cells. Cellular protrusions such as filopodia are known to provide a gateway for the entry of various viruses into a host cell. Myosin-2 (Lehmann et al., 2005) or myosin-6 (Sun and Whittaker, 2007) are indispensable for virus uptake. After multiplication the exit of virus particles from the infected cell again depend on Myosin-2A or B; examples are vaccinia virus (M. Way, London; personal communication to HOG) and herpes simplex virus (van Leeuwen, 2002)). Myosin-2A is furthermore required for the internalization of the CXCR4 receptor, which plays a role in HIV uptake into the cell. The uptake of the receptor can be inhibited by silencing nonmuscle myosin-2A with siRNA or using the myosin inhibitor blebbistatin (Rey et al, 2007). Furthermore, the release of HIV-1 from the host cell depends on myosin activity, since this process can be blocked with Wortmannin, an effective inhibitor of myosin light chain kinase (Sasaki et al., 1995). Based on these findings the inhibition of myosin activity is envisaged as an efficient treatment of viral infections. The fact that myosin plays a key role in viral spreading is reflected in the observation that even plant viruses (Tobacco mosaic virus, Kawakami et al., 2004) require myosin activity for spreading.

Members of the myosin superfamily are known to be involved in the host cell invasion of apicomplexan parasites. This group of protozoa includes species which are the cause of various human diseases of which malaria, toxoplasmosis or Eimeria infections are prominent examples. The gliding motility and invasion during infection depends on the activity of the unusual class-14, 23, and 24 myosins which is found in all Apicomplexa (Soldati et al., 2004).

Class-5 myosins are very abundant in the CNS (central nervous system) and mutations in the encoding gene give rise to severe neurological defects in mice and humans. In neurons, myosin-5a controls the targeting of IP3 (inositol 1,4,5-trisphosphate)-sensitive Ca²⁺ stores to dendritic spines and the transport of mRNAs (Desnos et. al., 2007). Whereas deletion of non-muscle myosins-2 A and B are accompanied by abnormalities in the brain and a defect in the migration of neuronal cells (facial neurons, cerebellar granule cell and pontine neurons (Kim et. al., 2005).

In a more preferred embodiment, said infection by parasites of Apicomplexa family is selected from malaria, toxoplasmosis and coccidiosis (e.g. by Eimeria).

In a more preferred embodiment, said cancer is selected from the group consisting of:

Anal Cancer (Squamous Cell Carcinoma of the Anus), Bladder Cancer (Squamous Cell Carcinoma of the Bladder), Bone Cancer (Chondrosarcoma of Cartilage), Osteosarcoma, Cancer of the bone marrow including Myelodysplastic syndrome (MDS), Acute Lymphoblastic Leukaemia (ALL), Promyelocytic Leukaemia (PML), Acute Myeloid Leukaemia (AML), Chronic Myeloid Leukaemia (CML), Chronic Lymphacytic Leukaemia (CLL), Multiple Myeloma, Brain Tumour including as Astrocytoma, Glioblastoma, Lymphoma of the Brain, Neuroblastoma, Breast Cancer including including Ductal Carcinoma of the Breast (DCIS) and Lobular Carcinoma of the Breast (LCIS), Bowel Cancer, Cervical Cancer, Colorectal Cancer including Adenocarcinoma of the Rectum and of the Colon, Head and Neck Cancer including Lymphoma of the Tonsil, Squamous Cell Carcinoma of the Floor of the Mouth (Oral Cancer), Squamous Cell Carcinoma of the Larynx, Pharynx, Tongue, and Squamous Cell Carcinoma of the Tonsil (Throat cancer), Kidney Cancer (Renal Cell Carcinoma), Liver Cancer (Hepatocellular Carcinoma), Lung Cancer including Malignant Mesothelioma of the Pleura (Malignant Mesothelioma), Adenocarcinoma of the Lung, Large Cell Carcinoma of the Lung, Non-small cell lung cancer (NSCLC), Small Cell Carcinoma of the Lung, Pleural effusion, Cancer of the Lymphatic System Hodgkin's lymphoma and non-Hodgkin's lymphoma including Anaplastic Large Cell Lymphoma (ALCL), Burkitt's lymphoma, Cerebral Lymphoma, Cutaneous T cell Lymphoma, Diffuse large B cell lymphoma (DLBCL), Muscle Cancer including Biliary Cancer (Cholangiocarcinoma), Leiomyosarcoma of Muscle, Rhabdomyosarcoma of Muscle, Soft tissue Sarcomas, Oesophagus Cancer, Ovarian Cancer, Pancreatic Cancer (Adenocarcinoma of the Pancreas), Pituitary gland Gland Cancer, Prostate Cancer including Neuroendocrine Carcinoma, Adenocarcinoma of the Prostate, Skin Cancer including Basal Cell Carcinoma of the Skin, Malignant Skin Melanoma, Small Intestine Cancer including Small Bowel cancer, Spinal Cord Tumours including Lymphoma, Astrocytoma, Glioma, Meningioma, and Metastases of the Spinal Cord, Stomach cancer, Testicular Cancer including Seminoma and Teratoma of the Testicle, Thyroid Cancer, Uterus Cancer (Adenocarcinoma of the Endometrium), Squamous Cell Carcinoma of the Vulva.

Viral infections according to the invention include infection by double-stranded DNA viruses such as viruses of Herpesviridae family include Herpes Simplex Virus (HSV). Furthermore deliberately envisaged are lentiviral and retroviral infections, including HIV infection (AIDS), Hepatitis-A, HBV (hepatitis-B) and HCV (hepatitis-C) infections.

Preferred diseases of the central nervous system (CNS) include:

Alzheimer Disease, Brain Ischemia, Cerebellar Ataxia, Cerebrovascular Accident, Corticobasal Ganglionic Degeneration (CBGD), Creutzfeldt-Jakob Syndrome, Dandy-Walker Syndrome, Dementia, Vascular, Encephalitis, Encephalomyelitis, Epilepsy, Hallervorden-Spatz Syndrome, Huntington Disease, Hydrocephalus, Ischemic Attack, Lacunar Syndromes, Landau-Kleffner Syndrome, Lewy Body Disease, Machado-Joseph Disease, Meige Syndrome, Meningitis, Multiple System Atrophy, Neuroaxonal Dystrophies, Parkinsonian Disorders, Shy-Drager Syndrome, Spinocerebellar Ataxias, Spinocerebellar Degenerations and Tourette Syndrome.

The present invention furthermore provides a compound of the following formula A-L-B, wherein A is selected from compounds of the general formulae (1) to (4) as defined above, L is a linker, B is blebbistatin or an analogue, and “—” is a covalent bond.

This embodiment provides divalent or multivalent compounds binding simultaneously to two or more binding sites of myosin. Such simultaneous binding to two or more binding sites may significantly enhance affinity and/or specificity. Blebbistatin as such has been described in the prior art; see e.g. Kovacs et al. (loc. cit.). Analogues of blebbistatin according to the invention are compounds binding to the blebbistatin binding pocket of myosins and/or exerting substantially the same modulating effect as blebbistatin. Blebbistatin interferes with myosin-2 function by inhibiting ATPase activity by blocking entry into the strong binding state, additionally it reduces the rate of ADP release. Preferred compounds A are carbazoles according to the invention (formulae (2) and (2′)). A preferred attachment site for the linker L on carbazoles according to the invention is the position Y₆. The linker L may be the substituent designated Y₆. Preferably the linker is a poly-methylene linker with four to eight, more preferred five to seven, most preferred six carbon atoms, i.e., —(CH₂)₆—. One or more CH₂ groups of said linker may be replaced with oxygen or sulphur. Accordingly, envisaged linkers include —O—(CH₂)₂—O—(CH₂)₂—. Further linkers are known in the art and can be used for the present invention, wherein it is preferred that the length of said linkers is the same or substantially the same as the length of a poly-methylene linker with four to eight, more preferred five to seven, most preferred six carbon atoms.

In preferred embodiments of the pharmaceutical composition, the use, or the compound of the formula A-L- Blebbistatin according to the invention, said one or more compounds or said compound A, respectively, are selected from compounds of the formulae (1′), (2′) and (3′):

wherein Y₁, Y₂, Y₃, Y₄, Y₅, Y₆, and Y₇ are independently selected from H, F, Cl, Br, I, R and OR; R being selected from (i) H, (ii) (CO)CH₃, and (iii) linear or branched alkyl, alkenyl or alkinyl with one to four carbon atoms, optionally substituted with one or more F, Cl, Br and/or I; or a salt or solvate thereof.

Preferably, Y₁ to Y₇, to the extent they are not H, are selected from Cl, Br, OCH₃ and CF₃. Particularly preferred are Br and CF₃.

In more preferred embodiments, (i) Y₁, Y₄ and Y₆ of formula (1′) are H; and/or (ii) Y₁, Y₄, Y₅ and Y₇ of formula (2′) are H.

In yet more preferred embodiments, furthermore (i) Y₇ of formula (1′) is H; and/or (ii) Y₂ of formula (2′) is H.

Accordingly, more preferred carbazoles include

More preferred acridones include

The preferred substitution patterns as defined in the preceding embodiments apply mutatis mutandis O- and S-analoga of the compounds of formulae (1′), and (3′), i.e., to the corresponding dibenzo-furans and dibenzo-thiophenes (O- and S-analoga of the compounds of formulae (1′)), as well as to the corresponding phenyl-furans and phenyl-thiophenes (O- and S-analoga of the compounds of formulae (3′)). Also these O- and S-analogs are embraced by the present invention. Accordingly, a preferred dibenzo-furan is

It is furthermore preferred that the substituents Y₁ to Y₇ on carbazoles, dibenzo-furans, dibenzo-thiophenes and acridones according to the invention, to the extent said substituents are present, i.e., different from H, are equal. Also, it is preferred that substituents Y₁, Y₂ and Y₃ of pseudilines, phenyl-furans and phenyl-thiophenes of the invention are equal. Furthermore, and independently, it is preferred that substituents Y₄ and Y₅ of said pseudilines, phenyl-furans and phenyl-thiophenes are equal. Preferably, said substituents which are equal are all Cl, Br, OCH₃ (herein also abbreviated “MeO”) or CF₃, respectively. Particularly preferred are Br and CF₃.

Further compounds of the invention are phenols which are substituted in positions 2, 4 and 6. Preferably, the substituents are selected from Br and CF₃. A preferred phenol according to the invention is 2,4,6-tribromo-phenol.

A further class of compounds according to the invention are fluorenes. Preferred fluorenes include 1-amino-9-hydroxy-fluorenes and 2-amino-9-hydroxy-fluorenes, which are optionally substituted, as valence permits, with one or more substituents selected from F, Cl, Br, I, R and OR; R being selected from (i) H, (ii) (CO)CH₃, and (iii) linear or branched alkyl, alkenyl or alkinyl with one to four carbon atoms, optionally substituted with one or more F, Cl, Br and/or I. A preferred fluorene according to the invention is 2-amino-3-bromo-9-hydroxy-fluorene.

Further preferred or exemplary compounds are shown below. These compounds—as are all compounds described herein—are inter alia envisaged as starting compounds far the method of designing according to the invention and as lead compounds which may be further optimized by using the lead optimization methods as described herein above. The “HET” series of compounds is herein also referred to as the “KIN” series of compounds. Accordingly, and as an example, “HET-43” and “KIN-43” designate the same compound.

HET-43 is also known as pentabromopseudilin (PBP).

The present invention furthermore provides a method of treating a disease selected from the group consisting of cardiovascular diseases, cancer, diseases of the central nervous system, viral infections, and infections by parasites of the Apicomplexa family, the method comprising administering to the subject in need thereof a therapeutically effective amount of one or more compounds as defined herein above.

Another embodiment of the invention is a method of treating a patient suffering from or at risk of developing a disease or condition selected from the group consisting of cardiovascular diseases, cancer, diseases of the central nervous system, viral infections, and infections by parasites of the Apicomplexa family, the method comprising administering to the patient a composition comprising one or more of the compounds defined above in a therapeutically effective dose, thereby treating the patient.

Preferred compounds and preferred indications to be treated or prevented by the above methods are described herein above in conjunction with medical uses and pharmaceutical compositions according to the invention.

The Figures show:

FIG. 1: Topology of myosin-2. Helices are shown as circles and beta-sheets as triangles.

FIG. 2: Sequence alignment of three representative myosins (Dictyostelium myosin-1E, Dictyostelium myosin-2 and Gallus gallus myosin-5). The ligand-binding sites are shaded. Dd=Dictyostefium discoideum, Gg=Gallus genus.

FIG. 3: Alignment of human myosin-2 isoforms. The isoforms are human myosins-2 from cardiac muscle, smooth muscle, non-muscle (NM) and brain tissue. The ligand-binding sites of the respective human myosins NM Myosin-MHC14, brain tissue-MHC15, cardiac alpha-MHC6, cardiac beta-MHC7, fast skeletal adult2-MHC2, fast skeletal embryonal-MHC3, skeletal adult1-MHC1, skeletal extraocular-MHC13, smooth muscle-MHC11, NM 2A-MHC9, NM 2B-MHC10 as compared to Dictyostelium myosin-2 (“MHCA Fulllength”) and MHC myosin heavy chain are shaded.

FIG. 4: Alignment of human and apicomplexan myosins. The ligand-binding sites of the respective human myosins cardiac beta-MHC7, fast skeletal adult2-MHC2, smooth muscle-MHC11, NM 2A-MHC9, NM 2B-MHC10 as compared to myosins-1 from Plasmodium falciparum (Pf MyoA und Pf MyoF), and from Toxoplasma gondii (Tg MYo A, Tg Myo B, Tg Myo E and Tg MyoG) are shaded. MHC=myosin heavy chain.

FIG. 5: Amino acid sequence pair distance of myosins from human, Apicomplexa and Dictyostelium. The underlying sequences are the sequence from amino acid 265 to 635 of Dd myosin and the corresponding subsequences of the other myosins aligning with this sequence.

FIG. 6: Histogram showing the relative myosin-2 ATPase activity measured in the absence (+control) and presence of halogenated alkaloids. Blebbistatin und BTS were used as controls. Compounds of the HET-series, BTS and blebbistatin were used at 25 μM final concentration. HET-43 is PBP (pentabromopseudilin). HET-68=pentachloropseudilin; Het-70=2,3,4-tribromo-5 (1′ hydroxy, 2′,4′-dichlorophenyl)pyrrole; Het-74=2,3,4-tribromo-5 (1′ hydroxy, 2′,4′-difluorophenyl)pyrrole; HET-76=2,3,4-triiodo-5 (1′ methoxy, 2′,4′-dichlorophenyl)pyrrole; HET-78=2,3,4-tribromo-5 (1′ methoxy, 2′,4′-diiodophenyl)pyrrole. The bars represent the mean value of three measurements. The error bars indicate the standard deviation.

FIG. 7: 2 Fo-Fc electron density omit map showing Het-43 (left) and the nucleotide (right) binding sites. The map was calculated using the final model of myosin-2(Het-43) complex with the inhibitor and the substrate omitted. The map was contoured at 1.0 σ.

Overall view of myosin(Het-43) complex (left). The details of Het-43 positioning in the binding site are shown in the close up (right). The transparent surface represents van-der-waals radii of the atoms forming Het-43 binding site.

FIG. 8: Comparison of the PBP-binding sites of Dictyostelium myosin-2, Dictyostelium myosin-1E, chicken myosin-5a, Saccharomyces cerevisiae myosin-2p, and Dictyostelium discoideum myosin-5b (from top to bottom).

FIG. 9: Inhibition of myosin functions by PBP. (a) Concentration-dependence of the inhibition of the actin-activated ATPase activity displayed by different myosin constructs. The semi-logarithmic plot shows the concentration dependence for myosin-1E (σ), myosin-2 (▪), and myosin-5b (Δ) from D. discoideum and for chicken myosin-5a (▾). (b) ATP turn-over rates of Dictyostelium myosin-2 (◯) and Dictyostelium myosin-5b (▪) at increasing F-actin concentrations in the absence (filled symbols) and presence (open symbols) of 25 μM pentabromopseudilin.

FIG. 10: ATP binding kinetics. For details see Example 2.

FIG. 11: (a) The histograms shows the average sliding velocity of Rh/Ph-labeled actin filaments in the absence and presence of 10 μM PBP. (b) Inhibition of chicken myosin-5a by PBP in the in vitro motility assay. The histograms show the average sliding velocity of Rh/Ph-labeled actin filaments in the absence and presence of 10 μM PBP. Myosin-5a moves actin filaments with an average velocity of 0.6 μm/s±0.05 (dark bars); addition of 10 μM PBP into the same flow cell decreases the average sliding velocity to 0.013 μm/s±0.002 (light grey bars).

FIG. 12: Isometric force measurements.

FIG. 13: Myo2p-dependent changes in mitochondrial morphology. In yeast cells, the class-5 myosins Myo2p is responsible for the distribution of mitochondria between mother and daughter cells during cytokinesis and has be shown to affect mitochondrial morphology during interface. (a) Wild-type yeast cells; (b) Myo2p-depleted cells; (a) the phenotype of Myo2p-depleted cells can be phenocopied by exposure of wild-type cells to 500 nM PBP. Insets show the same cells viewed under transmitted light. Bar: 5 μm

FIG. 14(A): Overview of HET-79 binding site. Het-79 binds bind in the same region and makes similar contacts as HET-43. However, there exist significant differences in the detailed interactions, the size of the contact area with the protein and the accessibility of the binding pocket.

FIG. 14(B): HET-79 binding pocket has three access channels. HET-79 binds in a pocket that is formed by residues at the interface between the 50 kDa upper domain (U50) and the 50 kDa lower domain (L50). The secondary structure elements that form the pocket include helix-13 (K265-V268), helix-21 (V411-L441), the strut loop (N588-Q593), loop 2 (D614-T629) and helix-29 (V630-E646). Both polar and apolar residues contribute to the binding of PBP. The HET-79 pocket has three major access channels. The first is located between loop-2 and the strut loop, the second is formed by residues from the loop connecting β7, the edge β-strand of the central β-sheet, with helix-13, helix-21, loop-2 and helix-29. The third is formed by residues from β7, helix-13, the loop connecting both, helix-21, and the strut loop.

FIG. 14(C): Detailed contacts with the OH-group of the carbazol derivative HET-79. K265 forms a hydrogen bond with the hydroxyl group. Additionally, K265 is in hydrogen bonding distance from a water molecule that is also in contact with D590. K423 and the carbonyl group of A424 form additional contacts with the OH-group of HET-79.

FIG. 14(D): Comparison with HET-43 Binding pocket.

FIG. 15(A): Het-68 (Pentachloropseudilin) binding shows major differences to that of the closely related pentabromopseudilin. Differences include major rearrangements of the loop-2 region, a reversal of the orientation of the inhibitor in the binding pocket, the complete planarity of HET-68, and its trans orientation of phenyl and pyrrol rings. Accordingly, there are also major changes in the contacts made between inhibitor and protein. K265 makes electrostatic interactions with the chlorine groups at positions 2 and 3 of the pyrrol ring; the chlorine in position 4 makes electrostatic interactions with D590. R428 forms a hydrogen bond with the OH group of the phenyl ring and the aliphatic part makes staggering interactions with pyrrol and phenyl ring. The aliphatic part of R620 makes a staggering interaction with the phenyl ring and its guanidinium group contributes an electrostatic interaction with the OH group. A618 and R620 form a tight indentation of the binding pocket that accommodates the 4′ chlorine, where the 4′ chlorine makes strong electrostatic interactions with the main chain amide groups of S619 and R620. Finally, E597 forms a hydrogen bond with a water molecule that is positioned close to the 2′ chlorine group of the phenyl ring.

FIG. 15(B): Overview of the Het-68 binding pocket. The second helix of the helix-loop-helix motif preceding loop-2 appears unstructured here and has moved closer towards the inhibitor. The inhibitor is completely planar and the binding pocket is more open towards the central β-sheet. The nucleotide binding pocket is seen in the lower-left corner.

FIG. 16: Cytotoxicity assay.

FIG. 17: ATPase activity assay.

FIG. 18: KIN-68-inhibition of the basal ATPase activity of Dictyostelium myosin-1E and myosin-5b. The concentrations of KIN-68 required for half-maximal inhibition of myosin-1E ATPase activity is 55.8 μM (a) and 104.6 μM for myosin-5b (b).

FIG. 19: Effects of KIN-74 and KIN-77 on the basal and actin-activated ATPase activity of Dictyostelium myosin-2 and rabbit myosin-2.

(a) Concentrations of KIN-7 in the range from 1 to 50 μM activate the basal ATPase activity of Dictyostelium myosin-2 with an apparent half maximum activation constant AC50 of 18 μM. At concentrations of KIN-74>50 μM the basal ATPase activity of Dictyostelium myosin-2 is inhibited with IC50=90 μM.

(b) In the presence of 30 μM actin KIN-74 inhibits the ATPase activity of Dictyostelium myosin-2 with IC50=88.8 μM

(c) KIN-77 inhibits the basal ATPase activity of myosin-2 approximately 3-fold with IC50=5.3 μM.

(d) Concentrations of KIN-77 in the range from 1 to 100 μM activate the basal ATPase activity of rabbit myosin-2 from 6.1 s-1 to 8.5 s-1 with a half maximum activation constant AC50=19.2 μM. At concentrations of KIN-77>100 μM the actin-activated ATPase activity of rabbit myosin-2 is inhibited 3.5-fold with an IC50=95.6 μM.

FIG. 20: (a) Plasmodium sporozoites adopt motility states, shown in the photos from the left to the right, attached, waving, clockwise (CW), and counterclockwise (CCW). In the absence of inhibitors sporozoites preferably move CW and CCW at 0.97 μm/s and 1.13 μm/s. (b) The addition of KIN-93 switched the population to attached and waving states and reduced the velocity for CW and CCW motility to 0.58 μm/s and 0.59 μm/s.

FIG. 21: Development toxicity testing of KIN-compounds on medaka embryos. (a) KIN-43 in concentrations between 0.5 μM and 100 μM were incubated for 48 h with 20 medaka embryos per concentration. The half lethal concentration of KIN-43 was at LC50=3.0 μM. (b) Light microscopy image of embryo after 48 h in the absence of KIN-43. (c) At higher concentration of KIN-43 the embryos agglomerate and die. (d) KIN-93 shows no lethal effect on medaka embryos in the lower micromolar range below 50.0 μM. LC50 is therefore well above a concentration of 50.0 μM.

FIG. 22: Cytotoxic testing of KIN-compounds by neutral red uptake assays. (a) human hepatocyte carcinoma cells (Hep G2) were exposed to KIN-43 for 4 h in the in presence of 1% FBS. KIN-43 shows a half effective concentration EC50 of 0.03 μM. (b) exposure of the same amount of KIN-93 did not show a measurable effect in the concentration range between 0.1 nM and 100 μM resulting in a LC50 well above a concentration of 50.0 μM.

The following examples illustrate the invention but should not be construed as being limiting.

EXAMPLE 1 Metal-Catalyzed Syntheses of Polyheterocyclic Compounds Introduction

Over the past two decades, applications of transition metals for selective C—H bond activation have emerged to a powerful tool in organic synthesis.

Methodologies have been developed for the cyclization of appropriately substituted primary or secondary alkyl- and arylamines, which open up simple and direct approaches to nitrogen-containing heterocyclic ring systems. These transformations are efficiently induced by using either stoichiometric or even catalytic amounts of transition metals (e.g., iron, molybdenum, palladium, or silver). The advantages of this synthetic approach are mild reaction conditions and toleration of a broad range of functional groups. Therefore, the construction of nitrogen-containing heterocyclic frameworks by fusion of fully functionalized building blocks is achieved in just a few synthetic steps. Application of this chemistry in heterocyclic synthesis provides convergent and highly efficient short-step approaches to a variety of biologically active compounds.¹

1. Silver(I)-Catalyzed Cyclization to Pyrroles

The pyrrole ring system represents a pivotal substructure in naturally occurring alkaloids and pharmaceutical products. Following the classical Hantzsch, Knorr, and Paal-Knorr syntheses numerous alternative assemblies of pyrroles have been reported. Homopropargylamines represent easily available building blocks for pyrrole synthesis. We recently described a novel pyrrole synthesis by silver(I)-mediated oxidative cyclization of homopropargylamines to pyrroles.² The required precursors are readily accessible by condensation of simple arylaldehydes to Schiff bases and subsequent Lewis acid-promoted addition of 3-trimethyl-silylpropargylmagnesium bromide (Scheme 1). Under optimized reaction conditions, treatment with 1.1 equivalents of silver acetate at room temperature affords the corresponding pyrroles almost quantitatively. This procedure represents a versatile and simple synthetic route to 1,2-diarylpyrroles, which are of interest due to their biological activities.

It is known that silver(I) salts form stable π-complexes with terminal acetylenes. On the other hand, silylacetylenes on treatment with silver nitrate were reported to afford silver acetylides. Based on these considerations and additional experimental evidence,² the following mechanistic rationale has been provided for the silver(I)-mediated oxidative cyclization of homopropargylamines to pyrroles (Scheme 2). Activation of the acetylene by coordination of the triple bond to the silver cation enables a 5-endo-dig cyclization via nucleophilic attack of the amine. Protonation of the resulting vinyl silver complex leads to an iminium ion. Subsequent β-hydride elimination affords metallic silver and a pyrrylium ion which aromatizes by proton loss to the pyrrole. For trimethylsilyl-substituted homopropargylamines (R³=SiMe₃), the resulting pyrrole (R³=SiMe₃) undergoes protodesilylation to the 1,2-disubstituted pyrrole.

Application: Synthesis of Pentabromopseudilin and Structural Analogues

Highly halogenated bioactive natural products as pentabromo- and pentachloropseudilin are often obtained from marine sources.³ For the construction of their heterocyclic framework a catalytic variant of our silver(I)-mediated pyrrole synthesis was applied: a silver(I)-catalyzed cyclization of the corresponding N-tosylhomopropargylamines (Scheme 3).

Starting from the appropriately substituted precursor, the dichloro- and the difluoro-O-methylpseudilin are available (Scheme 4). Further chlorination and subsequent cleavage of the ether provides pentachloropseudilin, while further bromination followed by ether cleavage leads to the non-natural dichlorotribromopseudilin and difluorotribromopseudilin. Our direct approach can be easily exploited for the generation of a whole series of structural analogues.

2. Transition Metal-Catalyzed Oxidative Cyclization to Carbazoles

A broad structural variety of carbazole alkaloids with useful biological activities has been isolated from different natural sources (Chinese and Indian medicinal plants, marine algae, streptomyces, etc.). The pharmacological potential of this class of natural products led to the development of diverse methodologies for the synthesis of carbazoles.⁴ We elaborated an efficient iron-mediated construction of the carbazole framework by consecutive C—C and C—N bond formation (Scheme 5). Electrophilic aromatic substitution by reaction of the iron-coordinated cyclohexadienylium salt 1 and the arylamine 2 generates the aryl-substituted iron-cyclohexadiene complex 3. Application of an appropriate oxidizing agent results in oxidative cyclization with concomitant aromatization and demetalation to afford directly the carbazole 4.

An alternative route to the carbazole framework represents the palladium(II)-catalyzed oxidative cyclization of N,N-diarylamines 6, which are readily available by palladium(0)-catalyzed amination of the aryl bromides 5 with the arylamines 2. Heating of the N,N-diarylamines 6 with catalytic amounts of palladium(II) acetate in the presence of copper(II) acetate in acetic acid at reflux results in smooth oxidative cyclization to the corresponding carbazoles 4 (Scheme 5).⁴

Application: Synthesis of Polybrominated 1-Hydroxycarbazoles

Using the palladium-catalyzed construction of the carbazole framework, an easy access to 1-methoxycarbazole has been achieved (Scheme 6). Dependent on the reagent and the reaction conditions, the subsequent bromination provides either 3,4,6-tribromo-1-methoxycarbazole or 3,4,6,8-tetrabromo-1-methoxycarbazole, which by cleavage of the ether are converted to the corresponding polybrominated 1-hydroxycarbazoles.

EXAMPLE 2 Allosteric Inhibition of Myosin Motor Activity by Pentabromopseudilin

The inventors surprisingly found several promising lead compounds; amongst them flavinoids and halogenated alkaloids; see FIG. 6. Furthermore, it was surprisingly found that pentabromopseudilin (PBP) was a very potent inhibitor of rabbit skeletal muscle heavy meromyosin (HMM) ATPase activity. The systematic name of PBP is 2,3,4-tribromo-5-(1′ hydroxy, 2′,4′-dibromophenyl)-pyrrole.

To identify the PBP binding site and to elucidate the inhibitory mechanism, we solved the cocrystal structure of PBP bound to the Dictyostelium myosin-2 motor domain. The structure shows the inhibitor to bind in a pocket close to the actin binding region at the tip of the 50-kDa domain. Based on the structure, we modeled the binding of PBP to Dictyostelium myosin-1E and chicken myosin-5a. Functional assays confirmed the predictions from the modeling that PBP is most potent as an inhibitor of class-5 myosins, less active for class-2 myosins, and displays weaker activity with class-1 myosins.

Identification of the PBP-Binding Site

To identify the binding mode of PBP, we crystallized the Dictyostelium myosin-2 motor domain MgATP-metavanadate complex in the presence and absence of PBP. We solved the complex structures by molecular replacement and refined them to 2.1 Å and 2.8 Å resolution, respectively. The overall fold of the motor domain in both structures is similar to that reported for the pre-powerstroke conformation. The α-carbon atoms in both structures superimpose with an r.m.s. deviation of 0.695. The electron density for PBP is unambiguous and shows the inhibitor in a conformation where the phenyl and pyrrole ring systems are bent by 12° out of plane and twisted by 20° against each other (FIG. 7). The inhibitor binds in a pocket that is formed by residues at the interphase between the 50 kDa upper domain (U50) and the 50 kDa lower domain (L50). The secondary structure elements that form the pocket include helix-13 (K265-V268), helix-21 (V411-L441), the strut loop (N588-Q593), loop 2 (D614-T629) and helix-29 (V630-E646). Both polar and apolar residues contribute to the binding of PBP. The pocket has a large opening that is surrounded by residues from loop-2, helix-29, the loop connecting β7, the edge β-strand of the central β-sheet, with helix-13, and helix-21. Additionally, a smaller access channel is located between loop-2 and the strut loop. The total protein surface area in contact with PBP comprises 255 Å².

Coordinates for the myosin-2 motor domain—ADP.VO₃ and myosin-2 motor domain—ADP.VO₃—PBP complexes have been deposited in the Protein Data Bank (PDB) with the accession codes 2JJ9 and 2JHR, respectively.

Binding of PBP requires several rearrangements of residues inside and near the binding pocket. The most extensive of these changes involve residue K265. To allow PBP to bind, the ammonium group of K265 needs to move 3.4 Å towards K423. The movement of K265 involves a change in rotamer and the stabilization of the side chain in its new position by an intricate network of interactions (FIG. 8). These include the formation of a key hydrogen bond with the hydroxyl group of the PBP phenol ring, a second hydrogen bond that is mediated via a water molecule from the ammonium group of K265 to the 2′-bromo group of phenyl ring, and contacts with the NH-group and the 2-bromo group of the pyrrol ring. Further stabilization is derived from a salt-bridge that forms between the ammonium group of K265 and the carboxyl group of D590. Formation of this salt-bridge requires a shift in the Cα-backbone at position D590. The side chains of A424, R428, and D590 and the main chain carbonyl of A420 and A618 are involved in the binding of the phenyl-ring, whereas the pyrrol ring has additional interactions with the side chain of L431 and the main chain carbonyl of I617. The carbonyl groups of I617 and A618 are in hydrogen-bonding distance to the bromo substituents in positions 3 and 4′, while the hydrogen bond between the carbonyl group of A420 and the 2′-bromo group is mediated by the same water molecule as the hydrogen bond between K265 and the hydroxyl group. The extent of side chain rearrangements associated with these interactions varies from 0.8 Å for L431 to 3.5 Å for R428. Residues R620 and Q633 are not in contact with PBP but their side chains undergo coordinated conformational changes, bringing them in positions were they form part of the large opening of the pocket. The guanidinium group moves 3.5 Å due to a 90° rotation around the Cδ-Cε bond, while a rotation around the Cα-Cβ bond leads to a 1.5 Å shift in the position of the side chain of Q633.

Specificity for Myosin Isoforms

Based on the structure of the myosin-2 motor domain with bound PBP, we performed molecular modeling studies to elucidate the specificity of PBP-binding to myosins from different classes. Here, we show the results for the modeling of complexes formed with class-1 and class-5 myosins, representing isoforms that are predicted to interact considerably stronger and weaker with the inhibitor (FIG. 8). The interaction between the lysine residue corresponding to K265 in myosin-2 is conserved in the other myosins. However, the number of interactions and their strength varies considerably between individual myosins. Myosin-1E is predicted to form only three hydrogen bonds and three weaker interactions, whereas myosin-5a is predicted to form twice as many interactions. To test the predictions from the modeling studies, we determined actin-activated ATPase activities in the presence of 0 to 150 μM PBP with rabbit skeletal myosin-2 heavy meromyosin (HMM), myosin-5a isolated from chicken brain, and recombinant Dictyostelium myosin class-1, 2 and 5 motor-domain constructs (FIG. 9 a). The semi-logarithmic plot shows the concentration dependence for myosin-1E (◯), myosin-2 (▪), myosin-5b (Δ) from D. discoideum, and for chicken myosin-5a (▾). The concentrations of PBP required for half-maximal inhibition of the different myosin motors was calculated from fitting the data to hyperbolae. The strongest inhibition was observed for chicken myosin-5a (K_(i)=1.19 μM±0.20), followed by Dictyostelium myosin-5b (K_(i)=19.3 μM±0.85), Dictyostelium myosin-2 (K_(i)=24 μM±1.5), HMM (K_(i)=23 μM±5), and Dictyostelium myosin-1E (K_(i)=49.5 μM±1.5) (FIG. 9 a). The ATPase activity at 30 μM F-actin decreased in the presence of >100 μM PBP for chicken myosin-5a from 8.5 s⁻¹ to 0.34 s⁻¹, for Dictyostelium myosin-5b from 5.5 s⁻¹ to 0.05 s⁻¹, for Dictyostelium myosin-2 from 0.7 s⁻¹ to 0.02 s⁻¹, and for Dictyostelium myosin-1E from 3.5 s⁻¹ to 0.10 s⁻¹. To determine the extend to which PBP impairs the coupling between the actin- and nucleotide-binding sites of myosin, we measured the ATP turn-over rates of Dictyostelium myosin-2 and myosin-5b motor domain constructs over the range from 0 to 50 μM F-actin in the absence and presence of 25 μM PBP.

Values for the rate of maximum ATP turnover (kcat), the concentration of F-actin at which half-maximal activation is achieved (Kapp), and the apparent second order rate constant for actin binding (kcat/Kapp) were estimated from a fit of the data to a hyperbolic function. kcat/Kapp is a direct measure of the coupling efficiency between actin and nucleotide binding and can be determined from the initial slope at F-actin concentrations much smaller than Kapp. Coupling was 26-fold weaker for myosin-5b (0.32 μM-1 s-1/0.012 μM-1 s-1), whereas a 3.7-fold reduction in coupling was observed for myosin-2 (0.037 μM-1 s-1/0.010 μM-1 s-1). ATP turn-over rates of Dictyostelium myosin-2 (◯) and Dictyostelium myosin-5b (▪) at increasing F-actin concentrations in the absence (filled symbols) and presence (open symbols) of 25 μM pentabromopseudilin (FIG. 9 b):

ATP Binding Kinetics

Effect of Pentabromopseudilin on ATP binding kinetics to DdMyosin-5b and acto-DdMyosin-5b. (FIG. 10 a) Fluorescence transients obtained upon mixing 1 μM DdMyosin-5b with 10 μM mantATP in the absence and presence of 5 μM, 25 μM, 50 μM and 100 μM PBP. Mant-fluorescence was excited at 365 nm and detected after passing through a KV 389 nm cut-off filter. The fluorescent signal of mantATP binding to DdMyosin-5b in the absence of PBP follows a single exponential function (upper curve). The presence of increasing concentrations of PBP lead to reduced amplitudes of the fluorescent signals that are best fit by double exponentials. (FIG. 10 b) Plot of the relative amplitudes of mantATP binding to Dd Myosin-5b at different PBP concentrations. A hyperbolic fit to the data yields an apparent constant K_(d) of 21±2 μM that is well consistent with the K_(i) value (19.14 μM) determined from the steady state ATPase measurements in FIG. 9 b. (FIG. 10 c) Fluorescence transients of the ATP induced dissociation of pyrene-acto-DdMyosin-5b in the absence (black curve) and presence (grey curve) of 50 μM PBP. (FIG. 10 d) Quench-flow experiments of the ATP hydrolysis reaction upon mixing 5 μM M761 with 25 μM ATP in the absence (solid squares) and presence (open circles) of 50 μM PBP. The P_(i)-burst (k_(burst)=7.8±0.2 sin the absence and 2.5±0.1 s⁻¹ in the presence of PBP) was followed by a linear steady-state phase. The amplitude of the burst was 0.95 in the absence and 0.5 in the presence of PBP.

The extent and order of isoform-specific differences in the potency of the inhibitor were additionally confirmed by the results of in vitro motility assays). The histograms shows the average sliding velocity of Rh/Ph-labeled actin filaments in the absence and presence of 10 μM PBP. (FIG. 11 a) Myosin-5a moves actin filaments with an average velocity of 0.6 μm/s±0.05 (dark bars); addition of 10 μM PBP into the same flow cell lead to a 46-fold reduction of the average sliding velocity to 0.013 μm/s±0.002 (light grey bars). A 2-to-3-fold reduction in the average gliding velocity was observed for myosin-2 at 100 μM PBP concentrations (FIG. 11 b). No significant inhibition was seen with myosin-1E (data not shown).

To test the effect of PBP on fully assembled myofilament arrays, we examined the contractile properties of skinned muscle fibre preparations from rabbit psoas muscle. Pentabromopseudilin leads to a more than 4-fold reduction in isometric force development of skinned muscle fibre preparations from rabbit psoas muscle. The Ki is in the same range as that determined for actomyosin ATPase activity. (FIG. 12)

Inhibition of Myosin-5-Dependent Cellular Processes

To test the specific inhibition of myosin-5 function in a cellular context, we exposed Saccharomyces cerevisiae cells to 100 to 500 nM PBP. S. cerevisiae has five myosin heavy chain genes: a myosin-2, two class-1 myosins, and the class-5 myosins Myo2p and Myo4p. Myo2p plays a crucial role in polarized distribution of mitochondria and is required for retention of newly inherited mitochondria in yeast cells during cell division⁴⁻⁶. Myo4p is required for mRNA transport and facilitates movement of ER tubules into the growing bud. Myo4p null mutants are viable and display no detectable phenotype. Deletion of the myo3 and myo5 genes, encoding class-1 myosins, leads to severe defects in growth and actin cytoskeletal organization. Severe growth defects are also observed upon depletion of the class-2 myosin Myo1p. Therefore, we expected that selective inhibition of class-5 myosins will produce readily detectable changes in the morphology of mitochondria without affecting cell growth and cytokinesis. To facilitate the visual inspection of mitochondrial morphology, we transfected the cells used for these experiments with an expression vector for the production of mitochondria-targeted GFP⁷. A yeast mutant strain with myo2 expression under the control of the TetO₇ promoter was used as control⁸. Repression of the TetO₇ promoter by the addition of 10 μg/ml deoxycycline to the culture medium of this strain led to an apparent fragmentation of mitochondria. Similar phenotypic changes were observed when wild-type cells were exposed to 500 nM PBP for 12 hours (FIG. 13 c). At lower concentrations the phenotype was less severe and at 100 nM PBP the mitochondrial morphology closely resembled that of untreated wild-type cells. Yeast cells exposed to 500 nM PBP showed similar growth kinetics as the wild type control cultures. These observations confirm the more potent inhibition of class-5 myosins observed the in vitro experiments and predicted by the in silica studies.

The results from the actin-activated ATPase measurements clearly demonstrate that PBP impairs the ability of myosins to effectively interact with nucleotides and actin; however the extent of inhibition by PBP is quite different for the individual myosins. The strongest inhibition was observed for class-5 myosins. In this case, the inhibitor caused a more than 25-fold increase in K_(app) and an approximately 8-fold decrease in k_(cat), while the same Michaelis-Menten parameters were less affected for a corresponding myosin-2 motor-domain construct.

Methods

Protein preparation. Rabbit fast skeletal muscle heavy meromyosin (HMM) was prepared as described by Kron and Spudich⁹. Motor domain constructs of myosin-1E, myosin-2, and myosin-5b from Dictyostelium discoideum comprising amino acids 1-698, 1-765, and 1-839 respectively, were prepared as described previouslyl¹⁰⁻¹². Myosin-5a heavy meromyosin from chicken brain was provided by Dr. T. Scholz (Hannover Medical School, Germany) and F-actin was prepared as described by Lehrer and Kerwar¹³.

Crystallization experiments were performed with myosin motor domain construct M761-c14 consisting of an N-terminal His-tag, amino acids 3 to 761 of myosin-2 from D. discoideum followed by a leucine and a glutamate residue and the 14 C-terminal residues of EcoSSB¹⁴. The protein was expressed in D. discoideum AX3-ORF+ cells and purified by Ni²⁺-chelate affinity chromatography as described previously¹⁵. Subsequently the protein was applied onto a Resource Q column (GE Healthcare) equilibrated with storage buffer (1 mM magnesium acetate, 0.5 mM EDTA, 0.2 mM EGTA, 1 mM benzamidine, 1 mM DTT, 50 mM Tris/HCl pH 7.5), followed by an elution with a gradient from 0 to 0.5 M KCl. The peak fractions were concentrated to 10 mg/ml using ultrafiltration (Vivaspin 20, Vivascience) and dialyzed against storage buffer containing 3% (w/v) sucrose. Aliquots of 100 μl were flash frozen in liquid nitrogen and stored at −80° C.

Synthesis of halogenated pseudilins. PBP and the other halogenated pseudilin derivates used in this study were synthesized using silver(I)-catalyzed pyrrole synthesis for the cyclization reaction to the heterocyclic system as described previously¹⁶.

Inhibitor screening. To screen compound libraries for myosin effectors, colorimetric high-throughput assays for myosin ATPase activity were performed with heavy meromyosin (HMM) prepared from rabbit skeletal muscle myosin-2. N_(α)-Tosyl-L-lysine chloromethyl ketone hydrochloride treated α-chymotrypsin was used for the generation of HMM. Each reaction mixture including the controls contained 2.5% DMSO that was used as solvent for the small organic compounds. Reactions containing HMM (0.01 mg/ml), assay buffer (50 mM KCl, 5 mM CaCl₂, 25 mM Tris-HCl pH 7.5) and 25 μM of the respective inhibitor were started by the addition of 50 μM ATP and incubated in for 20 min at 37° C. Reactions were terminated by the addition of Biomoi Green (Biomol, Hamburg, Germany). The amount of dye formed after 20 min color development at room temperature was determined with a Tecan Infinite™ microplate reader (Cralisheim, Germany).

Crystallization and data collection. The complex of M761-c14 with HET43 and ADP-VO₃ was obtained by adding 2 mM of PBP, MgCl₂, ADP and sodium meta-vanadate to the protein solution and incubation on ice for 1 hour. Crystals of the complex were grown in the dark at 4° C. using the hanging drop geometry. 2 μl of complex solution and 2 μl of reservoir solution were mixed, the latter contained 50 mM HEPES pH 7.4, 140 mM NaCl, 11% w/v PEG8000, 2% (v/v) MPD, 5 mM MgCl₂, 5 mM DTT, and 1 mM EGTA. Rectangular shaped crystals appeared within 3 weeks. Prior to diffraction data collection the crystals were soaked for 5 minutes at 4° C. in a cryo-protection solution containing reservoir solution supplemented with 25% ethylene glycol, 2 mM sodium meta-vanadate, 2 mM ADP and 2 mM HET43. Subsequently, crystals were flash-cooled in liquid nitrogen. Diffraction data were collected in house using a Bruker X8PROTEUM equipped with cryo-system, κ-goniometer and CCD-detector. We processed the data with PROTEUM2 software (Bruker AXS).

Molecular modeling. The motor domain structures of Dictyostelium myosin-1E (PDB entry 1 LKX) and chicken myosin-5A (PDB entry 1OE9) were used to model the complexes of class-1 and class-5 myosins with Het43. Initial models were created by inserting HET43 coordinates from superimposed myo2-HET43 complex. Next molecular mechanics energy minimization procedures were performed for HET43 in the new protein environment using the CNS software suit¹⁷. The resulting structures were subjected to a more precise quantum chemical energy minimization procedure, using ab initio DFT QM/MM calculations with the 6-31G* basis set of atomic orbitals and B3LYP hybrid functional. The quantum chemical calculations were performed using the PC GAMESS version developed by Alex A. Granovsky (http://www.classic.chem.msu.su/gran/gamess/index.html) of the GAMESS (US) Quantum Chemistry package¹⁸.

Steady-state kinetics. Basal and actin-activated Mg²⁺-ATPase activities were measured with the NADH-coupled assay¹⁹ in a buffer containing 25 mM HEPES, 25 mM KCl, and 4 mM MgCl₂, 0.5 mM DTT at pH 7.0 in the presence of 1 mM ATP at 25° C. PBP was added to the reaction mixture in the absence of nucleotide and incubated for 20 minutes before the reaction was started by the addition of ATP. NADH oxidation was followed using the change in absorption at 340 nm in a Beckman DU-800 spectrophotometer.

Transient kinetic experiments: Stopped-flow measurements were performed with an Applied Photophysics PiStar instrument in a buffer containing 25 mM HEPES, 25 mM KCl, 1 mM DTT, 4 mM MgCl₂, pH 7.0 at 20° C. using procedures and kinetic models described previously (1-3). The binding and hydrolysis of ATP and mantATP, respectively by myosin head fragments were analyzed in terms of the seven-step model described by Bagshaw and coworkers (4). Transients in the presence of actin were analyzed according to the mechanisms described in references 5 and 6.

Direct functional Assays. Actin-sliding motility was performed at 25° C. using an Olympus IX81 inverted fluorescence microscope. Experimental flow cells were constructed using bovine serum albumin (0.5 mg/ml in assay buffer)-coated glass slides and nitrocellulose-coated coverslips. Myosins were actin affinity-purified immediately before use, to remove rigor heads²⁰. Sliding movement was started by adding assay buffer containing 4 mM ATP, 10 mM DTT, 0.5 mg/ml bovine serum albumin, anti-fade solution, and 0.5% methylcellulose to the flow cell. Average sliding velocity was determined from the Gaussian distribution of automatically tracked actin filaments using DiaTrack 3.0 and Origin 7.0.

Quench-flow Experiments. Experiments were performed in a BioLogic QFM-400 apparatus. 20 μl of a 50 μM γ-³³P-ATP solution (0.3 μCi/μl) were mixed with an equal amount of 10 μM myosin solution in the absence and presence of 50 μM PBP in the assay buffer (25 mM HEPES, pH 7.3, 4 mM MgCl₂, 1 mM DTT, and 25 mM KCl at 25° C.). The reaction was quenched after a well defined period of time by the addition of 176 μl 1 M perchloric acid and rapidly neutralized by 60 μl of an 8 M KOAc. After centrifugation, 2 μl aliquots of the supernatant were spotted on a thin-layer chromatography (TLC) plate (Polygram CEL 300 PEI, cellose-molyethylenimin, Machery-Nagel). The hydrolysis products were separated in a 1.2 M LiCl solution containing 1 M HCOOH. The relative amounts of P₁ and ATP were quantified using a phosphorimager (Fujix BAS1000, Fuji), the software MacBAS V 2.4, TINA V 2.09f, and Origin 7.0.

Myo2p-dependent changes in mitochondrial morphology. The predicted strong inhibitory effect of PDP on myosin activity was tested in viva, making use of the phenotypic changes induced by the depletion of the class-5 myosin Myo2p in S. cerevisiae. Yeast strains producing mitochondria-targeted GFP were supplied by Dr. B. Westermann⁷, allowing us to study the morphology of yeast mitochondria in a fluorescence microscope. Repression of the TetO₇ promoter that controls myo2 in one of the mutant strains was achieved by the addition of 10 μg/ml deoxycycline to the culture medium⁸. Cells were analyzed at the end of the logarithmic growth phase. Yeast cells exposed to 500 nM PDP showed almost the same growth kinetics as wild type control cultures. Addition of 0.05% DMSO used as solvent vehicle for PBP had no effect on growth. Images of the mitochondrial phenotype were acquired using a Zeiss confocal microscope (LSM 510) equipped with a 63× oil immersion objective. Additional images of the same cells in transmitted light were acquired using a Hamamatsu ORCA camera.

TABLE 2 Data collection, structure solution and refinement statistics for the ternary myosin-2 motor domain - ADP• VO₃ - Pentabromopseudilin complex Myosin-2 - ADP•VO₃ - Complex Pentabromopseudilin Crystal parameters Group C222₁ Cell parameters: a, b, c; α, β, γ 89.8, 150.5, 154.6; 90, 90, 90 Data collection X-ray source X8PROTEUM, Bruker Wave length (Å)      1.54178 Resolution of data (Å)    2.8 No. of observations/ 134833/25708  unique reflections Completeness (total/high) % 98.2/95.5 <I/σ(I)> (total/high) 10.9/2.4  R_(sym) (total/high) %  8.8/40.4 Refinement Resolution range (Å) 8.0-2.8 Included amino acids 776 No. of protein atoms 6240  No. of waters 475 R_(work)/R_(free) % 21.7/26.5 r.m.s. deviation for bonds (Å)/angles 0.009/14   (deg)

EXAMPLE 3 Selectivity for Myosin Isoforms

KIN-43 shows preferred selectivity for mammalian myosin-5a, KIN-68 displays preferred selectivity for myosin-1 isoforms. In this context, preferred selectivity means a more than 20-fold smaller IC50 value compared to fast skeletal muscle myosin-2 and other references myosins.

EXAMPLE 4 Activators and Uncouplers of Myosin Function

Compounds KIN-74, KIN-77 are activators of myosin-2 function. KIN-74 activates the ATPase activity of Dictyostelium myosin-2 in the absence of actin. ATPase activity is uncoupled from motor activity in this situation. The apparent half-maximum activation constant AC₅₀ corresponds to 18 μM. Uncouplers have potential applications in inhibiting the overcontraction and overextension of cardiac muscles without being accompanied with a cardioinhibitory action. Therefore, compounds derived from KIN-74 have potential applications in the treatment of acute myocardial infarction helping to prevent the necrosis of cardiac muscles.

KIN-77 activates the actin-activated ATPase and motor activity of rabbit myosin-2 with a half maximum activation concentration AC₅₀=19.2 μM. KIN-77 is an ideal lead compounds for the development of optimized activators of myosin motor activity, Optimized activators have potential applications in diseases where myosin motility is impaired and contractility needs to be restored, as in the case of cardiomyopathies and congestive heart failures.

EXAMPLE 5 KIN-93 is an Inhibitor of Myosin-14-Dependet Motility in Plasmodium

Plasmodium sporozoites are moving at very low speed in the salivary glands of infected mosquitoes but are moving at high speed (2 μm/s) upon transmission into the vertebrate host. In vivo microscopy showed that sporozoites can move extensively within the dermis and when associated with blood and lymph vessels, which they can both invade. We followed single parasites using in vitro imaging approaches in combination with our bioactive compounds and discovered some intriguing features of sporozoite motility. Under normal conditions sporozoites move in circles, either counterclockwise or clockwise. Two other states of attachment and waving are less populated.

In the presence of 10 μM KIN-93, the number of sporozoite that followed counterclockwise or clockwise movement was strongly reduced. In addition, their gliding velocity was only half as fast as compared with control parasites. In addition to sporozoite impairment, in vitro growth assays indicate that the compound applied at concentration of 25 μM has an effect on the blood stages of malaria, too, by reducing the number of Plasmodium merozoites. No general cytotoxicity for erythrocytes or for Plasmodium sporozoites was recorded in any of the assays.

EXAMPLE 6 Optimization of Pharmacological Properties by In Silica Assisted Methods

Based on the X-ray structures of myosin-2 motor domains in complex with KIN-43 and related inhibitors of myosin function, we have gained a detailed understanding of the pharmacophore requirements of the allosteric binding site. By applying in silico assisted methods, we optimized the pharmacological properties of the initial bioactive compounds. We are using a library of common organic molecules and functional groups and are applying an empirical force field description of the nonbonding interactions between a ligand and the binding site in order to build up de novo compounds with spatial and electrostatic properties complementary to the allosteric binding site. KIN-93 is the result of a target directed drug design that shows improved pharmacological properties in relation to KIN-43. Cell viability is vastly improved in the presence of KIN-93. Neutral red uptake experiments do not reveal any defects. In addition, Medaka fish-based assays show that embryonic development is not impaired in the presence of KIN-93.

EXAMPLE 7 Structure of the Myosin-2-KIN79 Co-Crystal

The pdb coordinate file below shows the structure of the complex of the carbazole KIN-79 with myosin-2.

REMARK coordinates from minimization refinement REMARK refinement resolution: 500.0-2.2 A REMARK starting r = 0.3111 free_r = 0.3624 REMARK final r = 0.3067 free_r = 0.3617 REMARK rmsd bonds = 0.008031 rmsd angles = 1.30849 REMARK wa = 4.4505 REMARK target = mlf cycles = 1 steps = 200 REMARK sg = C222(1) a = 88.18 b = 149.90 c = 154.27 alpha = 90.0 beta = 90.0 gamma = 90 REMARK parameter file 1: CNS_TOPPAR: protein_rep.param REMARK parameter file 2: CNS_TOPPAR: ion.param REMARK parameter file 5: CNC_TOPPAR: water_rep.param REMARK molecular structure file: gen.mtf REMARK input coordinates: anneal_l.pdb REMARK reflection file = myo2het79.cv REMARK ncs = none REMARK B-correction resolution: 6.0-2.2 REMARK initial B-factor correction applied to fobs: REMARK B11 = 0.541 B22 = −12.873 B33 = 12.332 REMARK B12 = 0.000 B13 = 0.000 B23 = 0.000 REMARK B-factor correction applied to coordinate array B: −2.640 REMARK bulk solvent: density level = 0.319696 e/A{circumflex over ( )}3, B-factor = 33.6052 A{circumflex over ( )}2 REMARK reflections with |Fobs|/sigma_F < 0.0 rejected REMARK reflections with |Fobs| > 10000 * rms(Fobs) rejected REMARK theoretical total number of refl. in resol. range:  52178 (100.0%) REMARK number of unobserved reflections (no entry or |F| = 0):  81 (0.2%) REMARK number of reflections rejected:    0 (0.0%) REMARK total number of reflections used:    52097 (99.8%) REMARK number of reflections in working set:    49492 (94.9%) REMARK number of reflections in test set:    2605 (5.0%) CRYST1 88.180 149.900 154.270 90.00 90.00 90.00 C 2 2 21 ATOM 1 CB ASP 2 85.030 36.802 1.978 1.00 36.83 C ATOM 2 CG ASP 2 84.767 36.108 0.646 1.00 36.83 C ATOM 3 OD1 ASP 2 85.172 34.930 0.491 1.00 36.83 O ATOM 4 OD2 ASP 2 84.163 36.745 −0.251 1.00 36.83 O ATOM 5 C ASP 2 82.800 37.942 2.028 1.00 36.83 C ATOM 6 O ASP 2 82.248 37.200 2.832 1.00 36.83 O ATOM 7 N ASP 2 84.595 38.785 3.426 1.00 36.83 N ATOM 8 CA ASP 2 84.309 38.154 2.093 1.00 36.83 C ATOM 9 N PRO 3 82.116 38.612 1.083 1.00 36.83 N ATOM 10 CD PRO 3 82.704 39.658 0.232 1.00 36.83 C ATOM 11 CA PRO 3 80.667 38.545 0.865 1.00 36.83 C ATOM 12 CB PRO 3 80.481 39.420 −0.368 1.00 36.83 C ATOM 13 CG PRO 3 81.500 40.474 −0.136 1.00 36.83 C ATOM 14 C PRO 3 80.056 37.165 0.680 1.00 36.83 C ATOM 15 O PRO 3 79.024 36.853 1.268 1.00 36.83 O ATOM 16 N ILE 4 80.683 36.344 −0.154 1.00 36.83 N ATOM 17 CA ILE 4 80.178 35.003 −0.426 1.00 36.83 C ATOM 18 CB ILE 4 81.280 34.114 −1.051 1.00 36.83 C ATOM 19 CG2 ILE 4 80.701 32.766 −1.426 1.00 36.83 C ATOM 20 CG1 ILE 4 81.850 34.793 −2.297 1.00 36.83 C ATOM 21 CD1 ILE 4 83.126 34.159 −2.849 1.00 36.83 C ATOM 22 C ILE 4 79.619 34.284 0.811 1.00 36.83 C ATOM 23 O ILE 4 78.523 33.706 0.757 1.00 36.83 O ATOM 24 N HIS 5 80.351 34.337 1.924 1.00 36.83 N ATOM 25 CA HIS 5 79.938 33.634 3.141 1.00 36.83 C ATOM 26 CB HIS 5 81.126 32.885 3.730 1.00 36.83 C ATOM 27 CG HIS 5 81.702 31.857 2.807 1.00 36.83 C ATOM 28 CD2 HIS 5 82.836 31.858 2.065 1.00 36.83 C ATOM 29 ND1 HIS 5 81.060 30.667 2.530 1.00 36.83 N ATOM 30 CE1 HIS 5 81.774 29.980 1.654 1.00 36.83 C ATOM 31 NE2 HIS 5 82.856 30.679 1.354 1.00 36.83 N ATOM 32 C HIS 5 79.312 34.494 4.223 1.00 36.83 C ATOM 33 O HIS 5 78.933 33.995 5.285 1.00 36.83 O ATOM 34 N ASP 6 79.204 35.786 3.972 1.00 36.83 N ATOM 35 CA ASP 6 78.593 36.640 4.962 1.00 36.83 C ATOM 36 CB ASP 6 79.223 38.029 4.929 1.00 36.83 C ATOM 37 CG ASP 6 78.534 38.983 5.866 1.00 36.83 C ATOM 38 OD1 ASP 6 77.897 38.494 6.824 1.00 36.83 O ATOM 39 OD2 ASP 6 78.630 40.213 5.653 1.00 36.83 O ATOM 40 C ASP 6 77.088 36.726 4.703 1.00 36.83 C ATOM 41 O ASP 6 76.641 37.453 3.809 1.00 36.83 O ATOM 42 N ARG 7 76.315 35.979 5.489 1.00 36.83 N ATOM 43 CA ARG 7 74.858 35.968 5.341 1.00 36.83 C ATOM 44 CB ARG 7 74.229 34.940 6.293 1.00 36.83 C ATOM 45 CG ARG 7 74.983 33.603 6.376 1.00 36.83 C ATOM 46 CD ARG 7 74.044 32.479 6.807 1.00 36.83 C ATOM 47 NE ARG 7 74.709 31.205 7.106 1.00 36.83 N ATOM 48 CZ ARG 7 75.605 30.592 6.329 1.00 36.83 C ATOM 49 NH1 ARG 7 75.987 31.122 5.176 1.00 36.83 N ATOM 50 NH2 ARG 7 76.107 29.421 6.702 1.00 36.83 N ATOM 51 C ARG 7 74.229 37.336 5.602 1.00 36.83 C ATOM 52 O ARG 7 73.035 37.433 5.879 1.00 36.83 O ATOM 53 N THR 8 75.019 38.398 5.499 1.00 36.83 N ATOM 54 CA THR 8 74.489 39.731 5.773 1.00 36.83 C ATOM 55 CB THR 8 75.126 40.306 7.051 1.00 36.83 C ATOM 56 OG1 THR 8 76.469 40.716 6.773 1.00 36.83 O ATOM 57 CG2 THR 8 75.150 39.251 8.155 1.00 36.83 C ATOM 58 C THR 8 74.749 40.699 4.624 1.00 36.83 C ATOM 59 O THR 8 74.237 41.832 4.598 1.00 36.83 O ATOM 60 N SER 9 75.570 40.252 3.686 1.00 36.83 N ATOM 61 CA SER 9 75.920 41.070 2.537 1.00 36.83 C ATOM 62 CB SER 9 77.186 40.517 1.874 1.00 36.83 C ATOM 63 OG SER 9 76.976 39.205 1.376 1.00 36.83 O ATOM 64 C SER 9 74.779 41.078 1.525 1.00 36.83 C ATOM 65 O SER 9 73.923 40.186 1.538 1.00 36.83 O ATOM 66 N ASP 10 74.770 42.092 0.658 1.00 36.83 N ATOM 67 CA ASP 10 73.757 42.189 −0.388 1.00 36.83 C ATOM 68 CB ASP 10 74.066 43.369 −1.303 1.00 36.83 C ATOM 69 CG ASP 10 73.682 44.697 −0.691 1.00 36.83 C ATOM 70 OD1 ASP 10 74.272 45.716 −1.111 1.00 36.83 O ATOM 71 OD2 ASP 10 72.794 44.716 0.198 1.00 36.83 O ATOM 72 C ASP 10 73.780 40.905 −1.219 1.00 36.83 C ATOM 73 O ASP 10 72.753 40.447 −1.692 1.00 36.83 O ATOM 74 N TYR 11 74.973 40.354 −1.404 1.00 36.83 N ATOM 75 CA TYR 11 75.151 39.137 −2.172 1.00 36.83 C ATOM 76 CB TYR 11 76.631 38.731 −2.200 1.00 36.83 C ATOM 77 CG TYR 11 76.872 37.319 −2.685 1.00 36.83 C ATOM 78 CD1 TYR 11 76.866 36.246 −1.794 1.00 36.83 C ATOM 79 CE1 TYR 11 77.033 34.954 −2.230 1.00 36.83 C ATOM 80 CD2 TYR 11 77.060 37.050 −4.035 1.00 36.83 C ATOM 81 CE2 TYR 11 77.234 35.751 −4.487 1.00 36.83 C ATOM 82 CZ TYR 11 77.217 34.704 −3.579 1.00 36.83 C ATOM 83 OH TYR 11 77.364 33.410 −4.019 1.00 36.83 O ATOM 84 C TYR 11 74.304 38.001 −1.621 1.00 36.83 C ATOM 85 O TYR 11 73.816 37.172 −2.380 1.00 36.83 O ATOM 86 N HIS 12 74.133 37.955 −0.306 1.00 36.83 N ATOM 87 CA HIS 12 73.318 36.910 0.298 1.00 36.83 C ATOM 88 CB HIS 12 73.740 36.663 1.743 1.00 36.83 C ATOM 89 CG HIS 12 74.474 35.374 1.936 1.00 36.83 C ATOM 90 CD2 HIS 12 75.798 35.087 1.901 1.00 36.83 C ATOM 91 ND1 HIS 12 73.828 34.177 2.156 1.00 36.83 N ATOM 92 CE1 HIS 12 74.720 33.208 2.249 1.00 36.83 C ATOM 93 NE2 HIS 12 75.924 33.733 2.098 1.00 36.83 N ATOM 94 C HIS 12 71.849 37.279 0.243 1.00 36.83 C ATOM 95 O HIS 12 70.995 36.437 −0.073 1.00 36.83 O ATOM 96 N LYS 13 71.555 38.539 0.536 1.00 36.83 N ATOM 97 CA LYS 13 70.183 39.008 0.511 1.00 36.83 C ATOM 98 CB LYS 13 70.110 40.449 1.026 1.00 36.83 C ATOM 99 CG LYS 13 68.692 41.032 1.011 1.00 36.83 C ATOM 100 CD LYS 13 68.637 42.401 1.685 1.00 36.83 C ATOM 101 CE LYS 13 67.195 42.848 1.954 1.00 36.83 C ATOM 102 NZ LYS 13 67.078 44.178 2.674 1.00 36.83 N ATOM 103 C LYS 13 69.532 38.938 −0.880 1.00 36.83 C ATOM 104 O LYS 13 68.322 38.722 −0.985 1.00 36.83 O ATOM 105 N TYR 14 70.324 39.108 −1.943 1.00 36.83 N ATOM 106 CA TYR 14 69.755 39.113 −3.287 1.00 36.83 C ATOM 107 CB TYR 14 70.117 40.418 −4.002 1.00 36.83 C ATOM 108 CG TYR 14 69.593 41.634 −3.299 1.00 36.83 C ATOM 109 CD1 TYR 14 68.249 41.730 −2.968 1.00 36.83 C ATOM 110 CE1 TYR 14 67.751 42.845 −2.305 1.00 36.83 C ATOM 111 CD2 TYR 14 70.437 42.688 −2.950 1.00 36.83 C ATOM 112 CE2 TYR 14 69.950 43.807 −2.287 1.00 36.83 C ATOM 113 CZ TYR 14 68.607 43.876 −1.970 1.00 36.83 C ATOM 114 OH TYR 14 68.104 44.968 −1.324 1.00 36.83 O ATOM 115 C TYR 14 70.072 37.962 −4.216 1.00 36.83 C ATOM 116 O TYR 14 69.418 37.820 −5.252 1.00 36.83 O ATOM 117 N LEU 15 71.059 37.142 −3.870 1.00 36.83 N ATOM 118 CA LEU 15 71.419 36.032 −4.740 1.00 36.83 C ATOM 119 CB LEU 15 72.788 36.286 −5.346 1.00 36.83 C ATOM 120 CG LEU 15 72.827 37.366 −6.416 1.00 36.83 C ATOM 121 CD1 LEU 15 74.259 37.758 −6.708 1.00 36.83 C ATOM 122 CD2 LEU 15 72.131 36.843 −7.650 1.00 36.83 C ATOM 123 C LEU 15 71.411 34.667 −4.088 1.00 36.83 C ATOM 124 O LEU 15 71.684 33.671 −4.748 1.00 36.83 O ATOM 125 N LYS 16 71.097 34.617 −2.796 1.00 36.83 N ATOM 126 CA LYS 16 71.072 33.346 −2.073 1.00 36.83 C ATOM 127 CB LYS 16 72.095 33.365 −0.936 1.00 36.83 C ATOM 128 CG LYS 16 73.526 33.633 −1.388 1.00 36.83 C ATOM 129 CD LYS 16 74.077 32.499 −2.259 1.00 36.83 C ATOM 130 CE LYS 16 74.367 31.235 −1.441 1.00 36.83 C ATOM 131 NZ LYS 16 75.023 30.172 −2.258 1.00 36.83 N ATOM 132 C LYS 16 69.696 33.033 −1.507 1.00 36.83 C ATOM 133 O LYS 16 68.883 33.928 −1.267 1.00 36.83 O ATOM 134 N VAL 17 69.430 31.748 −1.306 1.00 36.83 N ATOM 135 CA VAL 17 68.154 31.334 −0.750 1.00 36.83 C ATOM 136 CB VAL 17 67.972 29.811 −0.894 1.00 36.83 C ATOM 137 CG1 VAL 17 66.852 29.318 0.016 1.00 36.83 C ATOM 138 CG2 VAL 17 67.674 29.479 −2.350 1.00 36.83 C ATOM 139 C VAL 17 68.110 31.733 0.719 1.00 36.83 C ATOM 140 O VAL 17 69.092 31.582 1.435 1.00 36.83 O ATOM 141 N LYS 18 66.964 32.246 1.155 1.00 36.83 N ATOM 142 CA LYS 18 66.783 32.676 2.535 1.00 36.83 C ATOM 143 CB LYS 18 65.436 33.389 2.705 1.00 36.83 C ATOM 144 CG LYS 18 65.220 34.625 1.810 1.00 36.83 C ATOM 145 CD LYS 18 65.595 35.925 2.535 1.00 36.83 C ATOM 146 CE LYS 18 64.914 37.145 1.896 1.00 36.83 C ATOM 147 NZ LYS 18 63.408 37.146 2.060 1.00 36.83 N ATOM 148 C LYS 18 66.824 31.494 3.496 1.00 36.83 C ATOM 149 O LYS 18 66.438 30.378 3.141 1.00 36.83 O ATOM 150 N GLN 19 67.293 31.761 4.714 1.00 36.83 N ATOM 151 CA GLN 19 67.376 30.766 5.780 1.00 36.83 C ATOM 152 CB GLN 19 68.059 31.387 6.995 1.00 36.83 C ATOM 153 CG GLN 19 68.183 30.476 8.200 1.00 36.83 C ATOM 154 CD GLN 19 69.015 29.239 7.924 1.00 36.83 C ATOM 155 OE1 GLN 19 70.071 29.319 7.296 1.00 36.83 O ATOM 156 NE2 GLN 19 68.547 28.085 8.404 1.00 36.83 N ATOM 157 C GLN 19 65.981 30.318 6.187 1.00 36.83 C ATOM 158 O GLN 19 65.125 31.145 6.487 1.00 36.83 O ATOM 159 N GLY 20 65.739 29.015 6.197 1.00 36.83 N ATOM 160 CA GLY 20 64.432 28.537 6.622 1.00 36.83 C ATOM 161 C GLY 20 64.331 28.631 8.142 1.00 36.83 C ATOM 162 O GLY 20 65.358 28.653 8.815 1.00 36.83 O ATOM 163 N ASP 21 63.118 28.702 8.692 1.00 36.83 N ATOM 164 CA ASP 21 62.968 28.775 10.143 1.00 36.83 C ATOM 165 CB ASP 21 61.783 29.664 10.541 1.00 36.83 C ATOM 166 CG ASP 21 60.478 29.245 9.877 1.00 36.83 C ATOM 167 OD1 ASP 21 60.138 28.040 9.902 1.00 36.83 O ATOM 168 OD2 ASP 21 59.777 30.129 9.329 1.00 36.83 O ATOM 169 C ASP 21 62.806 27.401 10.778 1.00 36.83 C ATOM 170 O ASP 21 62.915 26.368 10.109 1.00 36.83 O ATOM 171 N SER 22 62.528 27.395 12.076 1.00 36.83 N ATOM 172 CA SER 22 62.369 26.148 12.828 1.00 36.83 C ATOM 173 CB SER 22 62.186 26.436 14.325 1.00 36.83 C ATOM 174 OG SER 22 60.877 26.945 14.592 1.00 36.83 O ATOM 175 C SER 22 61.192 25.320 12.345 1.00 36.83 C ATOM 176 O SER 22 61.192 24.104 12.489 1.00 36.83 O ATOM 177 N ASP 23 60.183 25.976 11.789 1.00 36.83 N ATOM 178 CA ASP 23 59.011 25.258 11.309 1.00 36.83 C ATOM 179 CB ASP 23 57.848 26.234 11.099 1.00 36.83 C ATOM 180 CG ASP 23 57.414 26.915 12.406 1.00 36.83 C ATOM 181 OD1 ASP 23 57.735 28.110 12.612 1.00 36.83 O ATOM 182 OD2 ASP 23 56.765 26.241 13.234 1.00 36.83 O ATOM 183 C ASP 23 59.337 24.502 10.026 1.00 36.83 C ATOM 184 O ASP 23 58.957 23.337 9.868 1.00 36.83 O ATOM 185 N LEU 24 60.057 25.156 9.116 1.00 36.83 N ATOM 186 CA LEU 24 60.455 24.513 7.869 1.00 36.83 C ATOM 187 CB LEU 24 61.126 25.526 6.942 1.00 36.83 C ATOM 188 CG LEU 24 61.825 25.027 5.670 1.00 36.83 C ATOM 189 CD1 LEU 24 60.888 24.215 4.820 1.00 36.83 C ATOM 190 CD2 LEU 24 62.348 26.240 4.890 1.00 36.83 C ATOM 191 C LEU 24 61.414 23.352 8.170 1.00 36.83 C ATOM 192 O LEU 24 61.420 22.344 7.464 1.00 36.83 O ATOM 193 N PHE 25 62.222 23.487 9.216 1.00 36.83 N ATOM 194 CA PHE 25 63.148 22.414 9.579 1.00 36.83 C ATOM 195 CB PHE 25 63.989 22.798 10.805 1.00 36.83 C ATOM 196 CG PHE 25 64.918 21.709 11.278 1.00 36.83 C ATOM 197 CD1 PHE 25 64.538 20.846 12.302 1.00 36.83 C ATOM 198 CD2 PHE 25 66.160 21.526 10.681 1.00 36.83 C ATOM 199 CE1 PHE 25 65.381 19.810 12.726 1.00 36.83 C ATOM 200 CE2 PHE 25 67.006 20.497 11.096 1.00 36.83 C ATOM 201 CZ PHE 25 66.613 19.636 12.123 1.00 36.83 C ATOM 202 C PHE 25 62.354 21.143 9.863 1.00 36.83 C ATOM 203 O PHE 25 62.694 20.084 9.361 1.00 36.83 O ATOM 204 N LYS 26 61.290 21.255 10.652 1.00 36.83 N ATOM 205 CA LYS 26 60.446 20.103 10.975 1.00 36.83 C ATOM 206 CB LYS 26 59.250 20.524 11.838 1.00 36.83 C ATOM 207 CG LYS 26 59.616 21.164 13.166 1.00 36.83 C ATOM 208 CD LYS 26 58.378 21.683 13.896 1.00 36.83 C ATOM 209 CE LYS 26 58.724 22.260 15.277 1.00 36.83 C ATOM 210 NZ LYS 26 59.743 23.367 15.212 1.00 36.83 N ATOM 211 C LYS 26 59.923 19.428 9.709 1.00 36.83 C ATOM 212 O LYS 26 59.840 18.201 9.652 1.00 36.83 O ATOM 213 N LEU 27 59.560 20.226 8.701 1.00 36.83 N ATOM 214 CA LEU 27 59.045 19.679 7.437 1.00 36.83 C ATOM 215 CB LEU 27 58.291 20.735 6.617 1.00 36.83 C ATOM 216 CG LEU 27 57.044 21.461 7.131 1.00 36.83 C ATOM 217 CD1 LEU 27 56.485 22.239 5.947 1.00 36.83 C ATOM 218 CD2 LEU 27 55.963 20.499 7.669 1.00 36.83 C ATOM 219 C LEU 27 60.152 19.135 6.564 1.00 36.83 C ATOM 220 O LEU 27 59.890 18.374 5.643 1.00 36.83 O ATOM 221 N THR 28 61.387 19.524 6.846 1.00 36.83 N ATOM 222 CA THR 28 62.513 19.077 6.050 1.00 36.83 C ATOM 223 CB THR 28 63.659 20.114 6.079 1.00 36.83 C ATOM 224 OG1 THR 28 63.135 21.408 5.789 1.00 36.83 O ATOM 225 CG2 THR 28 64.726 19.772 5.054 1.00 36.83 C ATOM 226 C THR 28 63.054 17.727 6.505 1.00 36.83 C ATOM 227 O THR 28 63.621 16.995 5.696 1.0CG2 THR 28 O ATOM 228 N VAL 29 62.878 17.394 7.787 1.0CG2 THR 28 N ATOM 229 CA VAL 29 63.372 16.118 8.31R 1.0CG2 THR 28 C ATOM 230 CB VAL 29 63.974 16.254 9.749 1.0CG2 THR 28 C ATOM 231 CG1 VAL 29 65.13R 17.242 9.749 1.0CG2 THR 28 C ATOM 232 CG2 VAL 29 62.902 16.684 10.730 1.0CG2 THR 28 C ATOM 23R C VAL 29 62.282 15.057 8.357 1.0CG2 THR 28 C ATOM 234 O VAL 29 62.510 13.94R 8.799 1.0CG2 THR 28 O ATOM 235 N SER 30 61.091 15.409 7.909 1.0CG2 THR 28 N ATOM 236 CA SER 30 59.979 14.46R 7.89R 1.0CG2 THR 28 C ATOM 237 CB SER 30 58.746 15.146 7.298 1.0CG2 THR 28 C ATOM 238 OG SER 30 57.735 14.216 6.984 1.0CG2 THR 28 O ATOM 239 C SER 30 60.338 13.219 7.065 1.0CG2 THR 28 C ATOM 240 O SER 30 61.240 13.257 6.230 1.0CG2 THR 28 O ATOM 241 N ASP 31 59.627 12.121 7.296 1.0CG2 THR 28 N ATOM 242 CA ASP 31 59.879 10.89R 6.550 1.0CG2 THR 28 C ATOM 24R CB ASP 31 60.039 9.710 7.51R 1.0CG2 THR 28 C ATOM 244 CG ASP 31 61.329 9.800 8.337 1.0CG2 THR 28 C ATOM 245 OD1 ASP 31 61.252 10.144 9.545 1.0CG2 THR 28 O ATOM 246 OD2 ASP 31 62.429 9.546 7.767 1.0CG2 THR 28 O ATOM 247 C ASP 31 58.788 10.60R 5.519 1.0CG2 THR 28 C ATOM 248 O ASP 31 58.854 9.607 4.796 1.0CG2 THR 28 O ATOM 249 N LYS 32 57.791 11.481 5.44R 1.0CG2 THR 28 N ATOM 250 CA LYS 32 56.714 11.30R 4.47R 1.0CG2 THR 28 C ATOM 251 CB LYS 32 55.565 12.275 4.758 1.0CG2 THR 28 C ATOM 252 CG LYS 32 54.854 12.108 6.105 1.0CG2 THR 28 C ATOM 25R CD LYS 32 53.701 13.111 6.217 1.0CG2 THR 28 C ATOM 254 CE LYS 32 53.11R 13.162 7.629 1.0CG2 THR 28 C ATOM 255 NZ LYS 32 52.516 11.869 8.068 1.0CG2 THR 28 N ATOM 256 C LYS 32 57.237 11.565 3.055 1.0CG2 THR 28 C ATOM 257 O LYS 32 58.290 12.177 2.882 1.0CG2 THR 28 O ATOM 258 N ARG 3R 2856.4957 11.0957 2.050 1.0CG2 THR 28 N ATOM 259 CA ARG 3R 2856.87R 11.304 280.652 1.0CG2 THR 28 C ATOM 260 CB ARG 3R 2857.332 9.99R 0.018 1.0CG2 THR 28 C ATOM 261 CG ARG 3R 2858.4957 9.348 0.717 1.0CG2 THR 28 C ATOM 262 CD ARG 3R 2858.354 287THRR 0.645 1.0CG2 THR 28 C ATOM 26R NE ARG 3R 2858.370 7.377 −0.735 1.0CG2 THR 28 N ATOM 264 CZ ARG 3R 2859.485 7.097 −1.397 1.0CG2 THR 28 C ATOM 265 NH1 ARG 3R 2860.657 7.224 −0.782 1.0CG2 THR 28 N ATOM 266 NH2 ARG 3R 2859.435 6.71R −2.668 1.0CG2 THR 28 N ATOM 267 C ARG 3R 2855.671 11.866 −0.11R 1.0CG2 THR 28 C ATOM 268 O ARG 3R 2854.524 11.5HR 0.237 1.0CG2 THR 28 O ATOM 269 N TYR 34 55.940 12.657 −1.149 1.0CG2 THR 28 N ATOM 270 CA TYR 34 54.882 13.282 −1.930 1.0CG2 THR 28 C ATOM 271 CB TYR 34 54.805 14.775 −1.603 1.0CG2 THR 28 C ATOM 272 CG TYR 34 54.590 15.090 −0.136 1.0CG2 THR 28 C ATOM 27R CD1 TYR 34 55.638 14.990 0.786 1.0CG2 THR 28 C ATOM 274 CE1 TYR 34 55.435 15.258 2.141 1.0CG2 THR 28 C ATOM 275 CD2 TYR 34 53.338 15.466 0.33R 1.0CG2 THR 28 C ATOM 276 CE2 TYR 34 53.128 15.73R 1.685 1.0CG2 THR 28 C ATOM 277 CZ TYR 34 54.178 15.625 2.578 1.0CG2 THR 28 C ATOM 278 OH TYR 34 53.956 15.85R 3.914 1.0CG2 THR 28 O ATOM 279 C TYR 34 55.01R 13.109 −3.445 1.0CG2 THR 28 C ATOM 280 O TYR 34 56.078 12.784 −3.965 1.0CG2 THR 28 O ATOM 281 N ILE 35 53.911 13.352 −4.146 1.0CG2 THR 28 N ATOM 282 CA ILE 35 53.867 13.204 −5.592 1.0CG2 THR 28 C ATOM 28R CB ILE 35 53.11R 11.908 −5.981 1.0CG2 THR 28 C ATOM 284 CG2 ILE 35 51.64R 12.046 −5.644 1.0CG2 THR 28 C ATOM 285 CG1 ILE 35 53.284 11.614 −7.468 1.0CG2 THR 28 C ATOM 286 CD1 ILE 35 52.581 10.33R −7.917 1.0CG2 THR 28 C ATOM 287 C ILE 35 53.150 14.384 −6.231 1.0CG2 THR 28 C ATOM 288 O ILE 35 52.212 14.932 −5.649 1.0CG2 THR 28 O ATOM 289 N TRP 36 53.598 14.779 −7.420 1.0CG2 THR 28 N ATOM 290 CA TRP 36 52.960 15.877 −8.137 1.0CG2 THR 28 C ATOM 291 CB TRP 36 53.968 16.655 −8.989 1.0CG2 THR 28 C ATOM 292 CG TRP 36 54.920 17.507 −8.224 1.0CG2 THR 28 C ATOM 29R CD2 TRP 36 54.616 18.698 −7.477 1.0CG2 THR 28 C ATOM 294 CE2 TRP 36 55.828 19.169 −6.932 1.0CG2 THR 28 C ATOM 295 CE3 TRP 36 53.438 19.409 −7.215 1.0CG2 THR 28 C ATOM 296 CD1 TRP 36 56.264 17.317 −8.105 1.0CG2 THR 28 C ATOM 297 NE1 TRP 36 56.818 18.311 −7.33R 1.0CG2 THR 28 N ATOM 298 CZ2 TRP 36 55.899 20.322 −6.132 1.0CG2 THR 28 C ATOM 299 CZ3 TRP 36 53.507 20.556 −6.419 1.0CG2 THR 28 C ATOM 30CG CH2 TRP 36 54.731 20.998 −5.887 1.0CG2 THR 28 C ATOM 301 C TRP 36 51.937 15.231 −9.049 1.0CG2 THR 28 C ATOM 302 O TRP 36 52.262 14.287 −9.771 1.0CG2 THR 28 O ATOM 30R N TYR 37 50.699 15.717 −9.012 1.0CG2 THR 28 N ATOM 304 CA TYR 37 49.648 15.164 −9.868 1.0CG2 THR 28 C ATOM 305 CB TYR 37 48.792 14.18CG −9.072 1.0CG2 THR 28 C ATOM 306 CG TYR 37 47.94CG 14.852 −8.024G 1.0CG2 THR 28 C ATOM 307 CD1 TYR 37 48.492 15.305 −6THR1 1.0CG2 THR 28 C ATOM 308 CE1 TYR 37 47.727 16.019 −5.911 1.0CG2 THR 28 C ATOM 309 CD2 TYR 37 46.597 15.12CG −8.267 1.0CG2 THR 28 C ATOM 31CG CE2 TYR 37 45THR1 15TH29 −7.36R 1.0CG2 THR 28 C ATOM 311 CZ TYR 37 46.397 16.281 −6T190 1.0CG2 THR 28 C ATOM 312 OH TYR 37 45T632 17.019 −5.315 1.0CG2 THR 28 O ATOM 31R C TYR 37 48.77R 16.30CG −10.406 1.0CG2 THR 28 C ATOM 314 O TYR 37 48.878 17.43R −9.944 1.0CG2 THR 28 O ATOM 315 N ASN 38 47.909 15.994G −11.374 1.0CG2 THR 28 N ATOM 316 CA ASN 38 47.008 16.992 −11.962 1.00G2 THR 28 C ATOM 317 CB ASN 38 46.997 16.872 −13.496 1.00G2 THR 28 C ATOM 318 CG ASN 38 48.36R 17.095 −14.124 1.00G2 THR 28 C ATOM 319 OD1 ASN 38 48.946 18.169 −14.01R 1.00G2 THR 28 O ATOM 320 ND2 ASN 38 48.869 16.085 −14.79R 1.00G2 THR 28 N ATOM 321 C ASN 38 45.570 16.796 −11.449 1.00G2 THR 28 C ATOM 322 O ASN 38 44.939 15.7HR −11.737 1.00G2 THR 28 O ATOM 32R N PRO 39 45.039 17.762 −10.680 1.00G2 THR 28 N ATOM 324 CD PRO 39 45.695 18.976 −10.158 1.00G2 THR 28 C ATOM 325 CA PRO 39 43.672 17.649 −10.158 1.00G2 THR 28 C ATOM 326 CB PRO 39 43.469 18.977 −9.420 1.00G2 THR 28 C ATOM 327 CG PRO 39 44.850 19.29R −8.925 1.00G2 THR 28 C ATOM 328 C PRO 39 42.685 17.486 −11.304 1.00G2 THR 28 C ATOM 329 O PRO 39 41.777 16.659 −11.256 1.00G2 THR 28 O ATOM 330 N ASP 40 42.888 18.29CG −12.337 1.00G2 THR 28 N ATOM 331 CA ASP 40 42.046 18.278G −13.516 1.00G2 THR 28 C ATOM 332 CB ASP 40 41.660 19.711G −13.885 1.00G2 THR 28 C ATOM 33R CG ASP 40 40.686 19.776 −15.058 1.00G2 THR 28 C ATOM 334 OD1 ASP 40 40.760 18.904 −15.957 1.00G2 THR 28 O ATOM 335 OD2 ASP 40 39.859 20.719 −15.076 1.00G2 THR 28 O ATOM 336 C ASP 40 42.82R 17.639 −14.668 1.00G2 THR 28 C ATOM 337 O ASP 40 43.466 18.334 −15.450 1.00G2 THR 28 O ATOM 338 N PRO 41 42.752 16.303 −14.79R 1.00G2 THR 28 N ATOM 339 CD PRO 41 41.960 15.418G −13.915 1.00G2 THR 28 C ATOM 340 CA PRO 41 43.437 15.527G −15THR5 1.00G2 THR 28 C ATOM 341 CB PRO 41 42.75R 14.168 −15T749 1.00G2 THR 28 C ATOM 342 CG PRO 41 42.504 14.036 −14.252 1.00G2 THR 28 C ATOM 34R C PRO 41 43.416 16.114 −17.241 1.00G2 THR 28 C ATOM 344 O PRO 41 44.167 15.664 −18.111 1.00G2 THR 28 O ATOM 345 N LYS 42 42.562 17.107G −17.477 1.00G2 THR 28 N ATOM 346 CA LYS 42 42.511 17.735G −18.797 1.00G2 THR 28 C ATOM 347 CB LYS 42 41.132 18.346 −19.066 1.00G2 THR 28 C ATOM 348 CG LYS 42 40.048 17.299 −19.10R 1.00G2 THR 28 C ATOM 349 CD LYS 42 38.761 17.771G −19.72R 1.00G2 THR 28 C ATOM 350 CE LYS 42 37.785 16.585 −19.790 1.00G2 THR 28 C ATOM 351 NZ LYS 42 37.594 15.949 −18.442 1.00G2 THR 28 N ATOM 352 C LYS 42 43.584 18.813 −18.864 1.00G2 THR 28 C ATOM 35R O LYS 42 44.116 19.105 −19.942 1.00G2 THR 28 O ATOM 354 N GLU 4R 2843.895 19.392 −17.70R 1.00G2 THR 28 N ATOM 355 CA GLU 4R 2844.916 20.426 −17.582 1.00G2 THR 28 C ATOM 356 CB GLU 4R 2844.478 21.472 −16.558 1.00G2 THR 28 C ATOM 357 CG GLU 4R 2843.541 22.505 −17.152 1.00G2 THR 28 C ATOM 358 CD GLU 43 42.546 23.041 −16.142 1.00 36.83 C ATOM 359 OE1 GLU 43 42.982 23.604 −15.106 1.00 36.83 O ATOM 360 OE2 GLU 43 41.323 22.893 −16.391 1.00 36.83 O ATOM 361 C GLU 43 46.240 19.791 −17.162 1.00 36.83 C ATOM 362 O GLU 43 46.583 19.747 −15.974 1.00 36.83 O ATOM 363 N ARG 44 46.977 19.304 −18.154 1.00 36.83 N ATOM 364 CA ARG 44 48.263 18.647 −17.929 1.00 36.83 C ATOM 365 CB ARG 44 48.902 18.239 −19.274 1.00 36.83 C ATOM 366 CG ARG 44 48.144 17.183 −20.097 1.00 36.83 C ATOM 367 CD ARG 44 46.674 17.554 −20.343 1.00 36.83 C ATOM 368 NE ARG 44 46.472 18.772 −21.141 1.00 36.83 N ATOM 369 CZ ARG 44 46.410 18.808 −22.474 1.00 36.83 C ATOM 370 NH1 ARG 44 46.541 17.685 −23.183 1.00 36.83 N ATOM 371 NH2 ARG 44 46.192 19.966 −23.103 1.00 36.83 N ATOM 372 C ARG 44 49.282 19.477 −17.143 1.00 36.83 C ATOM 373 O ARG 44 50.054 18.923 −16.367 1.00 36.83 O ATOM 374 N ASP 45 49.288 20.793 −17.322 1.00 36.83 N ATOM 375 CA ASP 45 50.292 21.599 −16.626 1.00 36.83 C ATOM 376 CB ASP 45 50.797 22.711 −17.548 1.00 36.83 C ATOM 377 CG ASP 45 51.592 22.165 −18.724 1.00 36.83 C ATOM 378 OD1 ASP 45 52.490 21.320 −18.498 1.00 36.83 O ATOM 379 OD2 ASP 45 51.326 22.572 −19.870 1.00 36.83 O ATOM 380 C ASP 45 49.984 22.166 −15.250 1.00 36.83 C ATOM 381 O ASP 45 50.844 22.781 −14.627 1.00 36.83 O ATOM 382 N SER 46 48.774 21.958 −14.760 1.00 36.83 N ATOM 383 CA SER 46 48.429 22.439 −13.433 1.00 36.83 C ATOM 384 CB SER 46 46.950 22.776 −13.345 1.00 36.83 C ATOM 385 OG SER 46 46.643 23.196 −12.032 1.00 36.83 O ATOM 386 C SER 46 48.757 21.276 −12.505 1.00 36.83 C ATOM 387 O SER 46 48.253 20.169 −12.701 1.00 36.83 O ATOM 388 N TYR 47 49.604 21.525 −11.504 1.00 36.83 N ATOM 389 CA TYR 47 50.028 20.480 −10.582 1.00 36.83 C ATOM 390 CB TYR 47 51.538 20.241 −10.700 1.00 36.83 C ATOM 391 CG TYR 47 51.950 19.518 −11.957 1.00 36.83 C ATOM 392 CD1 TYR 47 51.916 18.126 −12.025 1.00 36.83 C ATOM 393 CE1 TYR 47 52.250 17.462 −13.187 1.00 36.83 C ATOM 394 CD2 TYR 47 52.333 20.224 −13.089 1.00 36.83 C ATOM 395 CE2 TYR 47 52.664 19.574 −14.253 1.00 36.83 C ATOM 396 CZ TYR 47 52.620 18.195 −14.295 1.00 36.83 C ATOM 397 OH TYR 47 52.935 17.551 −15.456 1.00 36.83 O ATOM 398 C TYR 47 49.713 20.780 −9.146 1.00 36.83 C ATOM 399 O TYR 47 49.826 21.915 −8.694 1.00 36.83 O ATOM 400 N GLU 48 49.320 19.741 −8.424 1.00 36.83 N ATOM 401 CA GLU 48 49.018 19.880 −7.012 1.00 36.83 C ATOM 402 CB GLU 48 47.544 19.578 −6.752 1.00 36.83 C ATOM 403 CG GLU 48 47.144 19.915 −5.347 1.00 36.83 C ATOM 404 CD GLU 48 47.430 21.370 −5.011 1.00 36.83 C ATOM 405 OE1 GLU 48 46.559 22.233 −5.313 1.00 36.83 O ATOM 406 OE2 GLU 48 48.530 21.643 −4.461 1.00 36.83 O ATOM 407 C GLU 48 49.924 18.880 −6.287 1.00 36.83 C ATOM 408 O GLU 48 50.539 18.028 −6.930 1.00 36.83 O ATOM 409 N CYS 49 50.027 18.988 −4.967 1.00 36.83 N ATOM 410 CA CYS 49 50.892 18.077 −4.226 1.00 36.83 C ATOM 411 CB CYS 49 51.881 18.876 −3.367 1.00 36.83 C ATOM 412 SG CYS 49 53.037 17.882 −2.388 1.00 36.83 S ATOM 413 C CYS 49 50.082 17.118 −3.360 1.00 36.83 C ATOM 414 O CYS 49 49.276 17.544 −2.543 1.00 36.83 O ATOM 415 N GLY 50 50.294 15.816 −3.551 1.00 36.83 N ATOM 416 CA GLY 50 49.572 14.823 −2.770 1.00 36.83 C ATOM 417 C GLY 50 50.504 13.930 −1.965 1.00 36.83 C ATOM 418 O GLY 50 51.619 13.619 −2.397 1.00 36.83 O ATOM 419 N GLU 51 50.059 13.513 −0.785 1.00 36.83 N ATOM 420 CA GLU 51 50.891 12.658 0.047 1.00 36.83 C ATOM 421 CB GLU 51 50.540 12.836 1.530 1.00 36.83 C ATOM 422 CG GLU 51 51.304 11.891 2.451 1.00 36.83 C ATOM 423 CD GLU 51 51.060 12.163 3.928 1.00 36.83 C ATOM 424 OE1 GLU 51 51.547 11.371 4.774 1.00 36.83 O ATOM 425 OE2 GLU 51 50.384 13.170 4.244 1.00 36.83 O ATOM 426 C GLU 51 50.743 11.188 −0.338 1.00 36.83 C ATOM 427 O GLU 51 49.638 10.702 −0.574 1.00 36.83 O ATOM 428 N ILE 52 51.865 10.488 −0.426 1.00 36.83 N ATOM 429 CA ILE 52 51.820 9.068 −0.738 1.00 36.83 C ATOM 430 CB ILE 52 53.169 8.546 −1.213 1.00 36.83 C ATOM 431 CG2 ILE 52 53.147 7.022 −1.254 1.00 36.83 C ATOM 432 CG1 ILE 52 53.479 9.117 −2.598 1.00 36.83 C ATOM 433 CD1 ILE 52 54.809 8.658 −3.161 1.00 36.83 C ATOM 434 C ILE 52 51.421 8.317 0.525 1.00 36.83 C ATOM 435 O ILE 52 52.185 8.254 1.485 1.00 36.83 O ATOM 436 N VAL 53 50.215 7.761 0.521 1.00 36.83 N ATOM 437 CA VAL 53 49.708 7.016 1.669 1.00 36.83 C ATOM 438 CB VAL 53 48.169 7.082 1.736 1.00 36.83 C ATOM 439 CG1 VAL 53 47.720 8.531 1.782 1.00 36.83 C ATOM 440 CG2 VAL 53 47.559 6.378 0.538 1.00 36.83 C ATOM 441 C VAL 53 50.125 5.541 1.677 1.00 36.83 C ATOM 442 O VAL 53 50.265 4.945 2.736 1.00 36.83 O ATOM 443 N SER 54 50.331 4.951 0.505 1.00 36.83 N ATOM 444 CA SER 54 50.722 3.547 0.441 1.00 36.83 C ATOM 445 CB SER 54 49.515 2.665 0.711 1.00 36.83 C ATOM 446 OG SER 54 48.657 2.695 −0.414 1.00 36.83 O ATOM 447 C SER 54 51.288 3.174 −0.919 1.00 36.83 C ATOM 448 O SER 54 51.346 3.999 −1.842 1.00 36.83 O ATOM 449 N GLU 55 51.700 1.918 −1.059 1.00 36.83 N ATOM 450 CA GLU 55 52.241 1.482 −2.331 1.00 36.83 C ATOM 451 CB GLU 55 53.658 2.029 −2.505 1.00 36.83 C ATOM 452 CG GLU 55 54.770 1.122 −2.038 1.00 36.83 C ATOM 453 CD GLU 55 56.053 1.877 −1.846 1.00 36.83 C ATOM 454 OE1 GLU 55 56.241 2.451 −0.757 1.00 36.83 O ATOM 455 OE2 GLU 55 56.873 1.921 −2.785 1.00 36.83 O ATOM 456 C GLU 55 52.248 −0.029 −2.510 1.00 36.83 C ATOM 457 O GLU 55 52.349 −0.788 −1.545 1.00 36.83 O ATOM 458 N THR 56 52.112 −0.450 −3.760 1.00 36.83 N ATOM 459 CA THR 56 52.150 −1.861 −4.097 1.00 36.83 C ATOM 460 CB THR 56 51.040 −2.253 −5.088 1.00 36.83 C ATOM 461 OG1 THR 56 51.226 −1.530 −6.312 1.00 36.83 O ATOM 462 CG2 THR 56 49.663 −1.924 −4.523 1.00 36.83 C ATOM 463 C THR 56 53.483 −2.011 −4.795 1.00 36.83 C ATOM 464 O THR 56 54.333 −1.113 −4.748 1.00 36.83 O ATOM 465 N SER 57 53.659 −3.138 −5.462 1.00 36.83 N ATOM 466 CA SER 57 54.901 −3.415 −6.180 1.00 36.83 C ATOM 467 CB SER 57 54.908 −4.872 −6.630 1.00 36.83 C ATOM 468 OG SER 57 56.205 −5.254 −7.036 1.00 36.83 O ATOM 469 C SER 57 55.112 −2.513 −7.403 1.00 36.83 C ATOM 470 O SER 57 56.244 −2.190 −7.746 1.00 36.83 O ATOM 471 N ASP 58 54.027 −2.122 −8.067 1.00 36.83 N ATOM 472 CA ASP 58 54.145 −1.276 −9.257 1.00 36.83 C ATOM 473 CB ASP 58 53.771 −2.069 −10.524 1.00 36.83 C ATOM 474 CG ASP 58 52.272 −2.337 −10.631 1.00 36.83 C ATOM 475 OD1 ASP 58 51.501 −1.715 −9.877 1.00 36.83 O ATOM 476 OD2 ASP 58 51.850 −3.161 −11.478 1.00 36.83 O ATOM 477 C ASP 58 53.285 −0.022 −9.216 1.00 36.83 C ATOM 478 O ASP 58 52.963 0.527 −10.262 1.00 36.83 O ATOM 479 N SER 59 52.883 0.429 −8.037 1.00 36.83 N ATOM 480 CA SER 59 52.044 1.619 −7.988 1.00 36.83 C ATOM 481 CB SER 59 50.595 1.266 −8.339 1.00 36.83 C ATOM 482 OG SER 59 50.020 0.426 −7.350 1.00 36.83 O ATOM 483 C SER 59 52.071 2.350 −6.663 1.00 36.83 C ATOM 484 O SER 59 52.517 1.826 −5.642 1.00 36.83 O ATOM 485 N PHE 60 51.599 3.586 −6.710 1.00 36.83 N ATOM 486 CA PHE 60 51.543 4.454 −5.547 1.00 36.83 C ATOM 487 CB PHE 60 52.364 5.736 −5.758 1.00 36.83 C ATOM 488 CG PHE 60 53.839 5.591 −5.529 1.00 36.83 C ATOM 489 CD1 PHE 60 54.331 5.121 −4.320 1.00 36.83 C ATOM 490 CD2 PHE 60 54.740 6.020 −6.494 1.00 36.83 C ATOM 491 CE1 PHE 60 55.701 5.084 −4.075 1.00 36.83 C ATOM 492 CE2 PHE 60 56.107 5.990 −6.262 1.00 36.83 C ATOM 493 CZ PHE 60 56.589 5.523 −5.055 1.00 36.83 C ATOM 494 C PHE 60 50.108 4.886 −5.388 1.00 36.83 C ATOM 495 O PHE 60 49.386 5.044 −6.369 1.00 36.83 O ATOM 496 N THR 61 49.704 5.073 −4.143 1.00 36.83 N ATOM 497 CA THR 61 48.377 5.560 −3.837 1.00 36.83 C ATOM 498 CB THR 61 47.573 4.538 −3.029 1.00 36.83 C ATOM 499 OG1 THR 61 47.180 3.469 −3.897 1.00 36.83 O ATOM 500 CG2 THR 61 46.345 5.178 −2.424 1.00 36.83 C ATOM 501 C THR 61 48.613 6.821 −3.013 1.00 36.83 C ATOM 502 O THR 61 49.282 6.785 −1.989 1.00 36.83 O ATOM 503 N PHE 62 48.094 7.943 −3.475 1.00 36.83 N ATOM 504 CA PHE 62 48.291 9.186 −2.750 1.00 36.83 C ATOM 505 CB PHE 62 49.152 10.147 −3.581 1.00 36.83 C ATOM 506 CG PHE 62 48.593 10.435 −4.946 1.00 36.83 C ATOM 507 CD1 PHE 62 48.825 9.569 −6.011 1.00 36.83 C ATOM 508 CD2 PHE 62 47.827 11.580 −5.171 1.00 36.83 C ATOM 509 CE1 PHE 62 48.300 9.843 −7.290 1.00 36.83 C ATOM 510 CE2 PHE 62 47.302 11.860 −6.432 1.00 36.83 C ATOM 511 CZ PHE 62 47.539 10.993 −7.495 1.00 36.83 C ATOM 512 C PHE 62 46.980 9.858 −2.383 1.00 36.83 C ATOM 513 O PHE 62 45.923 9.506 −2.890 1.00 36.83 O ATOM 514 N LYS 63 47.066 10.826 −1.482 1.00 36.83 N ATOM 515 CA LYS 63 45.914 11.586 −1.037 1.00 36.83 C ATOM 516 CB LYS 63 46.003 11.845 0.474 1.00 36.83 C ATOM 517 CG LYS 63 45.425 10.730 1.323 1.00 36.83 C ATOM 518 CD LYS 63 45.177 11.190 2.748 1.00 36.83 C ATOM 519 CE LYS 63 44.258 10.216 3.478 1.00 36.83 C ATOM 520 NZ LYS 63 42.925 10.111 2.806 1.00 36.83 N ATOM 521 C LYS 63 45.909 12.924 −1.771 1.00 36.83 C ATOM 522 O LYS 63 46.927 13.613 −1.796 1.00 36.83 O ATOM 523 N THR 64 44.780 13.301 −2.365 1.00 36.83 N ATOM 524 CA THR 64 44.718 14.594 −3.056 1.00 36.83 C ATOM 525 CB THR 64 43.515 14.684 −3.982 1.00 36.83 C ATOM 526 OG1 THR 64 42.320 14.781 −3.195 1.00 36.83 O ATOM 527 CG2 THR 64 43.446 13.456 −4.867 1.00 36.83 C ATOM 528 C THR 64 44.587 15.701 −2.010 1.00 36.83 C ATOM 529 O THR 64 44.545 15.416 −0.805 1.00 36.83 O ATOM 530 N VAL 65 44.536 16.960 −2.444 1.00 36.83 N ATOM 531 CA VAL 65 44.393 18.045 −1.471 1.00 36.83 C ATOM 532 CB VAL 65 44.744 19.435 −2.064 1.00 36.83 C ATOM 533 CG1 VAL 65 46.265 19.608 −2.129 1.00 36.83 C ATOM 534 CG2 VAL 65 44.124 19.587 −3.436 1.00 36.83 C ATOM 535 C VAL 65 42.956 18.056 −0.991 1.00 36.83 C ATOM 536 O VAL 65 42.695 18.097 0.214 1.00 36.83 O ATOM 537 N ASP 66 42.026 18.000 −1.941 1.00 36.83 N ATOM 538 CA ASP 66 40.609 17.980 −1.611 1.00 36.83 C ATOM 539 CB ASP 66 39.763 17.779 −2.880 1.00 36.83 C ATOM 540 CG ASP 66 40.464 16.929 −3.932 1.00 36.83 C ATOM 541 OD1 ASP 66 41.622 17.262 −4.289 1.00 36.83 O ATOM 542 OD2 ASP 66 39.855 15.939 −4.415 1.00 36.83 O ATOM 543 C ASP 66 40.343 16.871 −0.588 1.00 36.83 C ATOM 544 O ASP 66 39.457 17.006 0.271 1.00 36.83 O ATOM 545 N GLY 67 41.116 15.785 −0.672 1.00 36.83 N ATOM 546 CA GLY 67 40.962 14.695 0.277 1.00 36.83 C ATOM 547 C GLY 67 40.545 13.337 −0.261 1.00 36.83 C ATOM 548 O GLY 67 39.916 12.557 0.466 1.00 36.83 O ATOM 549 N GLN 68 40.874 13.042 −1.518 1.00 36.83 N ATOM 550 CA GLN 68 40.522 11.746 −2.107 1.00 36.83 C ATOM 551 CB GLN 68 40.130 11.895 −3.572 1.00 36.83 C ATOM 552 CG GLN 68 38.644 11.811 −3.859 1.00 36.83 C ATOM 553 CD GLN 68 37.915 13.116 −3.592 1.00 36.83 C ATOM 554 OE1 GLN 68 37.887 13.613 −2.456 1.00 36.83 O ATOM 555 NE2 GLN 68 37.319 13.682 −4.644 1.00 36.83 N ATOM 556 C GLN 68 41.705 10.777 −2.021 1.00 36.83 C ATOM 557 O GLN 68 42.670 11.007 −1.280 1.00 36.83 O ATOM 558 N ASP 69 41.613 9.696 −2.789 1.00 36.83 N ATOM 559 CA ASP 69 42.653 8.674 −2.842 1.00 36.83 C ATOM 560 CB ASP 69 42.285 7.460 −1.991 1.00 36.83 C ATOM 561 CG ASP 69 43.019 7.431 −0.671 1.00 36.83 C ATOM 562 OD1 ASP 69 43.006 6.363 0.001 1.00 36.83 O ATOM 563 OD2 ASP 69 43.599 8.464 −0.295 1.00 36.83 O ATOM 564 C ASP 69 42.835 8.227 −4.272 1.00 36.83 C ATOM 565 O ASP 69 42.029 7.468 −4.812 1.00 36.83 O ATOM 566 N ARG 70 43.894 8.704 −4.897 1.00 36.83 N ATOM 567 CA ARG 70 44.155 8.323 −6.264 1.00 36.83 C ATOM 568 CB ARG 70 44.460 9.545 −7.129 1.00 36.83 C ATOM 569 CG ARG 70 43.283 10.478 −7.350 1.00 36.83 C ATOM 570 CD ARG 70 43.630 11.473 −8.439 1.00 36.83 C ATOM 571 NE ARG 70 42.673 12.574 −8.533 1.00 36.83 N ATOM 572 CZ ARG 70 42.803 13.585 −9.384 1.00 36.83 C ATOM 573 NH1 ARG 70 43.841 13.620 −10.204 1.00 36.83 N ATOM 574 NH2 ARG 70 41.910 14.561 −9.404 1.00 36.83 N ATOM 575 C ARG 70 45.339 7.391 −6.271 1.00 36.83 C ATOM 576 O ARG 70 46.169 7.416 −5.362 1.00 36.83 O ATOM 577 N GLN 71 45.414 6.590 −7.321 1.00 36.83 N ATOM 578 CA GLN 71 46.466 5.624 −7.478 1.00 36.83 C ATOM 579 CB GLN 71 45.828 4.232 −7.476 1.00 36.83 C ATOM 580 CG GLN 71 46.776 3.054 −7.267 1.00 36.83 C ATOM 581 CD GLN 71 46.016 1.758 −6.982 1.00 36.83 C ATOM 582 OE1 GLN 71 45.087 1.390 −7.713 1.00 36.83 O ATOM 583 NE2 GLN 71 46.411 1.058 −5.915 1.00 36.83 N ATOM 584 C GLN 71 47.131 5.916 −8.817 1.00 36.83 C ATOM 585 O GLN 71 46.481 6.420 −9.733 1.00 36.83 O ATOM 586 N VAL 72 48.424 5.615 −8.925 1.00 36.83 N ATOM 587 CA VAL 72 49.164 5.818 −10.170 1.00 36.83 C ATOM 588 CB VAL 72 49.690 7.265 −10.284 1.00 36.83 C ATOM 589 CG1 VAL 72 50.599 7.581 −9.111 1.00 36.83 C ATOM 590 CG2 VAL 72 50.443 7.440 −11.591 1.00 36.83 C ATOM 591 C VAL 72 50.345 4.851 −10.256 1.00 36.83 C ATOM 592 O VAL 72 50.938 4.492 −9.239 1.00 36.83 O ATOM 593 N LYS 73 50.674 4.422 −11.474 1.00 36.83 N ATOM 594 CA LYS 73 51.780 3.492 −11.693 1.00 36.83 C ATOM 595 CB LYS 73 51.790 3.020 −13.158 1.00 36.83 C ATOM 596 CG LYS 73 50.681 2.019 −13.528 1.00 36.83 C ATOM 597 CD LYS 73 51.029 0.592 −13.049 1.00 36.83 C ATOM 598 CE LYS 73 49.845 −0.360 −13.187 1.00 36.83 C ATOM 599 NZ LYS 73 49.171 −0.238 −14.523 1.00 36.83 N ATOM 600 C LYS 73 53.117 4.154 −11.349 1.00 36.83 C ATOM 601 O LYS 73 53.296 5.357 −11.550 1.00 36.83 O ATOM 602 N LYS 74 54.058 3.374 −10.831 1.00 36.83 N ATOM 603 CA LYS 74 55.360 3.922 −10.475 1.00 36.83 C ATOM 604 CB LYS 74 56.201 2.867 −9.754 1.00 36.83 C ATOM 605 CG LYS 74 55.772 2.660 −8.322 1.00 36.83 C ATOM 606 CD LYS 74 56.617 1.618 −7.600 1.00 36.83 C ATOM 607 CE LYS 74 56.226 1.567 −6.122 1.00 36.83 C ATOM 608 NZ LYS 74 56.991 0.588 −5.311 1.00 36.83 N ATOM 609 C LYS 74 56.114 4.465 −11.685 1.00 36.83 C ATOM 610 O LYS 74 56.831 5.465 −11.590 1.00 36.83 O ATOM 611 N ASP 75 55.941 3.795 −12.819 1.00 36.83 N ATOM 612 CA ASP 75 56.582 4.188 −14.059 1.00 36.83 C ATOM 613 CB ASP 75 56.432 3.069 −15.091 1.00 36.83 C ATOM 614 CG ASP 75 57.442 1.940 −14.884 1.00 36.83 C ATOM 615 OD1 ASP 75 57.371 0.925 −15.631 1.00 36.83 O ATOM 616 OD2 ASP 75 58.308 2.075 −13.983 1.00 36.83 O ATOM 617 C ASP 75 56.007 5.489 −14.620 1.00 36.83 C ATOM 618 O ASP 75 56.614 6.108 −15.495 1.00 36.83 O ATOM 619 N ASP 76 54.844 5.903 −14.123 1.00 36.83 N ATOM 620 CA ASP 76 54.214 7.133 −14.594 1.00 36.83 C ATOM 621 CB ASP 76 52.828 6.842 −15.174 1.00 36.83 C ATOM 622 CG ASP 76 52.889 6.007 −16.443 1.00 36.83 C ATOM 623 OD1 ASP 76 53.603 6.398 −17.400 1.00 36.83 O ATOM 624 OD2 ASP 76 52.216 4.958 −16.485 1.00 36.83 O ATOM 625 C ASP 76 54.073 8.191 −13.509 1.00 36.83 C ATOM 626 O ASP 76 53.414 9.208 −13.723 1.00 36.83 O ATOM 627 N ALA 77 54.686 7.966 −12.353 1.00 36.83 N ATOM 628 CA ALA 77 54.571 8.926 −11.266 1.00 36.83 C ATOM 629 CB ALA 77 54.695 8.210 −9.913 1.00 36.83 C ATOM 630 C ALA 77 55.565 10.076 −11.330 1.00 36.83 C ATOM 631 O ALA 77 56.680 9.931 −11.814 1.00 36.83 O ATOM 632 N ASN 78 55.130 11.229 −10.847 1.00 36.83 N ATOM 633 CA ASN 78 55.983 12.408 −10.783 1.00 36.83 C ATOM 634 CB ASN 78 55.288 13.609 −11.408 1.00 36.83 C ATOM 635 CG ASN 78 55.225 13.519 −12.897 1.00 36.83 C ATOM 636 OD1 ASN 78 56.244 13.375 −13.560 1.00 36.83 O ATOM 637 ND2 ASN 78 54.028 13.612 −13.439 1.00 36.83 N ATOM 638 C ASN 78 56.255 12.694 −9.315 1.00 36.83 C ATOM 639 O ASN 78 55.655 13.595 −8.732 1.00 36.83 O ATOM 640 N GLN 79 57.142 11.912 −8.713 1.00 36.83 N ATOM 641 CA GLN 79 57.465 12.104 −7.308 1.00 36.83 C ATOM 642 CB GLN 79 58.452 11.029 −6.829 1.00 36.83 C ATOM 643 CG GLN 79 57.817 9.665 −6.597 1.00 36.83 C ATOM 644 CD GLN 79 58.737 8.695 −5.883 1.00 36.83 C ATOM 645 OE1 GLN 79 59.590 8.053 −6.495 1.00 36.83 O ATOM 646 NE2 GLN 79 58.569 8.589 −4.579 1.00 36.83 N ATOM 647 C GLN 79 58.062 13.484 −7.075 1.00 36.83 C ATOM 648 O GLN 79 58.739 14.039 −7.946 1.00 36.83 O ATOM 649 N ARG 80 57.785 14.043 −5.905 1.00 36.83 N ATOM 650 CA ARG 80 58.329 15.340 −5.561 1.00 36.83 C ATOM 651 CB ARG 80 57.384 16.097 −4.638 1.00 36.83 C ATOM 652 CG ARG 80 57.962 17.411 −4.129 1.00 36.83 C ATOM 653 CD ARG 80 56.932 18.215 −3.362 1.00 36.83 C ATOM 654 NE ARG 80 57.533 19.404 −2.763 1.00 36.83 N ATOM 655 CZ ARG 80 56.853 20.343 −2.117 1.00 36.83 C ATOM 656 NH1 ARG 80 55.537 20.236 −1.978 1.00 36.83 N ATOM 657 NH2 ARG 80 57.492 21.395 −1.621 1.00 36.83 N ATOM 658 C ARG 80 59.651 15.126 −4.857 1.00 36.83 C ATOM 659 O ARG 80 59.826 14.174 −4.103 1.00 36.83 O ATOM 660 N ASN 81 60.595 16.010 −5.110 1.00 36.83 N ATOM 661 CA ASN 81 61.889 15.910 −4.466 1.00 36.83 C ATOM 662 CB ASN 81 62.893 16.834 −5.166 1.00 36.83 C ATOM 663 CG ASN 81 63.421 16.238 −6.457 1.00 36.83 C ATOM 664 OD1 ASN 81 64.034 15.168 −6.448 1.00 36.83 O ATOM 665 ND2 ASN 81 63.182 16.918 −7.570 1.00 36.83 N ATOM 666 C ASN 81 61.769 16.293 −3.001 1.00 36.83 C ATOM 667 O ASN 81 60.845 16.998 −2.617 1.00 36.83 O ATOM 668 N PRO 82 62.670 15.777 −2.153 1.00 36.83 N ATOM 669 CD PRO 82 63.571 14.636 −2.397 1.00 36.83 C ATOM 670 CA PRO 82 62.629 16.123 −0.728 1.00 36.83 C ATOM 671 CB PRO 82 63.868 15.429 −0.178 1.00 36.83 C ATOM 672 CG PRO 82 63.884 14.155 −0.984 1.00 36.83 C ATOM 673 C PRO 82 62.741 17.639 −0.685 1.00 36.83 C ATOM 674 O PRO 82 63.448 18.217 −1.496 1.00 36.83 O ATOM 675 N ILE 83 62.068 18.298 0.245 1.00 36.83 N ATOM 676 CA ILE 83 62.124 19.743 0.242 1.00 36.83 C ATOM 677 CB ILE 83 61.062 20.362 1.183 1.00 36.83 C ATOM 678 CG2 ILE 83 59.687 19.800 0.833 1.00 36.83 C ATOM 679 CG1 ILE 83 61.398 20.098 2.645 1.00 36.83 C ATOM 680 CD1 ILE 83 61.284 18.651 3.045 1.00 36.83 C ATOM 681 C ILE 83 63.491 20.348 0.509 1.00 36.83 C ATOM 682 O ILE 83 63.663 21.560 0.376 1.00 36.83 O ATOM 683 N LYS 84 64.470 19.524 0.860 1.00 36.83 N ATOM 684 CA LYS 84 65.800 20.062 1.095 1.00 36.83 C ATOM 685 CB LYS 84 66.718 19.042 1.793 1.00 36.83 C ATOM 686 CG LYS 84 67.093 17.813 0.972 1.00 36.83 C ATOM 687 CD LYS 84 68.260 17.094 1.648 1.00 36.83 C ATOM 688 CE LYS 84 68.358 15.624 1.269 1.00 36.83 C ATOM 689 NZ LYS 84 68.567 1.5.414 −0.183 1.00 36.83 N ATOM 690 C LYS 84 66.385 20.471 −0.256 1.00 36.83 C ATOM 691 O LYS 84 67.387 21.157 −0.317 1.00 36.83 O ATOM 692 N PHE 85 65.736 20.051 −1.338 1.00 36.83 N ATOM 693 CA PHE 85 66.176 20.389 −2.691 1.00 36.83 C ATOM 694 CB PHE 85 65.914 19.232 −3.649 1.00 36.83 C ATOM 695 CG PHE 85 66.951 18.156 −3.607 1.00 36.83 C ATOM 696 CD1 PHE 85 68.206 18.358 −4.170 1.00 36.83 C ATOM 697 CD2 PHE 85 66.669 16.927 −3.030 1.00 36.83 C ATOM 698 CE1 PHE 85 69.174 17.344 −4.162 1.00 36.83 C ATOM 699 CE2 PHE 85 67.626 15.909 −3.016 1.00 36.83 C ATOM 700 CZ PHE 85 68.878 16.120 −3.583 1.00 36.83 C ATOM 701 C PHE 85 65.448 21.624 −3.220 1.00 36.83 C ATOM 702 O PHE 85 65.779 22.133 −4.287 1.00 36.83 O ATOM 703 N ASP 86 64.455 22.107 −2.491 1.00 36.83 N ATOM 704 CA ASP 86 63.730 23.278 −2.957 1.00 36.83 C ATOM 705 CB ASP 86 62.426 23.460 −2.171 1.00 36.83 C ATOM 706 CG ASP 86 61.362 22.434 −2.562 1.00 36.83 C ATOM 707 OD1 ASP 86 60.229 22.511 −2.047 1.00 36.83 O ATOM 708 OD2 ASP 86 61.658 21.544 −3.385 1.00 36.83 O ATOM 709 C ASP 86 64.578 24.544 −2.894 1.00 36.83 C ATOM 710 O ASP 86 64.846 25.082 −1.820 1.00 36.83 O ATOM 711 N GLY 87 65.002 25.003 −4.068 1.00 36.83 N ATOM 712 CA GLY 87 65.796 26.210 −4.149 1.00 36.83 C ATOM 713 C GLY 87 67.174 25.924 −4.682 1.00 36.83 C ATOM 714 O GLY 87 67.900 26.850 −5.028 1.00 36.83 O ATOM 715 N VAL 88 67.526 24.639 −4.748 1.00 36.83 N ATOM 716 CA VAL 88 68.835 24.210 −5.221 1.00 36.83 C ATOM 717 CB VAL 88 68.809 22.698 −5.601 1.00 36.83 C ATOM 718 CG1 VAL 88 68.352 22.508 −7.037 1.00 36.83 C ATOM 719 CG2 VAL 88 70.166 22.080 −5.360 1.00 36.83 C ATOM 720 C VAL 88 69.296 25.075 −6.401 1.00 36.83 C ATOM 721 O VAL 88 68.489 25.497 −7.234 1.00 36.83 O ATOM 722 N GLU 89 70.592 25.347 −6.468 1.00 36.83 N ATOM 723 CA GLU 89 71.136 26.196 −7.524 1.00 36.83 C ATOM 724 CB GLU 89 72.428 26.844 −7.043 1.00 36.83 C ATOM 725 CG GLU 89 72.323 27.456 −5.668 1.00 36.83 C ATOM 726 CD GLU 89 73.542 28.267 −5.333 1.00 36.83 C ATOM 727 OE1 GLU 89 74.666 27.827 −5.684 1.00 36.83 O ATOM 728 OE2 GLU 89 73.372 29.341 −4.724 1.00 36.83 O ATOM 729 C GLU 89 71.396 25.505 −8.851 1.00 36.83 C ATOM 730 O GLU 89 71.405 26.142 −9.890 1.00 36.83 O ATOM 731 N ASP 90 71.609 24.198 −8.802 1.00 36.83 N ATOM 732 CA ASP 90 71.887 23.414 −9.989 1.00 36.83 C ATOM 733 CB ASP 90 73.310 22.864 −9.900 1.00 36.83 C ATOM 734 CG ASP 90 73.838 22.381 −11.228 1.00 36.83 C ATOM 735 OD1 ASP 90 73.079 21.707 −11.951 1.00 36.83 O ATOM 736 OD2 ASP 90 75.020 22.669 −11.542 1.00 36.83 O ATOM 737 C ASP 90 70.880 22.271 −9.986 1.00 36.83 C ATOM 738 O ASP 90 70.969 21.366 −9.158 1.00 36.83 O ATOM 739 N MET 91 69.925 22.313 −10.909 1.00 36.83 N ATOM 740 CA MET 91 68.891 21.290 −10.977 1.00 36.83 C ATOM 741 CB MET 91 67.754 21.757 −11.887 1.00 36.83 C ATOM 742 CG MET 91 67.139 23.064 −11.404 1.00 36.83 C ATOM 743 SD MET 91 65.634 23.513 −12.244 1.00 36.83 S ATOM 744 CE MET 91 66.263 23.836 −13.851 1.00 36.83 C ATOM 745 C MET 91 69.404 19.916 −11.398 1.00 36.83 C ATOM 746 O MET 91 68.636 18.962 −11.475 1.00 36.83 O ATOM 747 N SER 92 70.705 19.819 −11.658 1.00 36.83 N ATOM 748 CA SER 92 71.321 18.543 −12.020 1.00 36.83 C ATOM 749 CB SER 92 72.785 18.752 −12.441 1.00 36.83 C ATOM 750 OG SER 92 72.882 19.624 −13.550 1.00 36.83 O ATOM 751 C SER 92 71.304 17.644 −10.784 1.00 36.83 C ATOM 752 O SER 92 71.316 16.420 −10.888 1.00 36.83 O ATOM 753 N GLU 93 71.275 18.283 −9.620 1.00 36.83 N ATOM 754 CA GLU 93 71.292 17.622 −8.326 1.00 36.83 C ATOM 755 CB GLU 93 71.771 18.616 −7.272 1.00 36.83 C ATOM 756 CG GLU 93 73.171 19.159 −7.478 1.00 36.83 C ATOM 757 CD GLU 93 73.498 20.276 −6.494 1.00 36.83 C ATOM 758 OE1 GLU 93 73.371 20.075 −5.266 1.00 36.83 O ATOM 759 OE2 GLU 93 73.877 21.372 −6.956 1.00 36.83 O ATOM 760 C GLU 93 69.992 16.985 −7.824 1.00 36.83 C ATOM 761 O GLU 93 70.015 16.270 −6.816 1.00 36.83 O ATOM 762 N LEU 94 68.873 17.251 −8.500 1.00 36.83 N ATOM 763 CA LEU 94 67.576 16.723 −8.088 1.00 36.83 C ATOM 764 CB LEU 94 66.465 17.288 −8.976 1.00 36.83 C ATOM 765 CG LEU 94 66.157 18.787 −8.927 1.00 36.83 C ATOM 766 CD1 LEU 94 65.115 19.101 −9.967 1.00 36.83 C ATOM 767 CD2 LEU 94 65.666 19.193 −7.544 1.00 36.83 C ATOM 768 C LEU 94 67.501 15.204 −8.122 1.00 36.83 C ATOM 769 O LEU 94 67.918 14.591 −9.093 1.00 36.83 O ATOM 770 N SER 95 66.955 14.602 −7.068 1.00 36.83 N ATOM 771 CA SER 95 66.822 13.150 −7.015 1.00 36.83 C ATOM 772 CB SER 95 66.207 12.697 −5.690 1.00 36.83 C ATOM 773 OG SER 95 66.693 13.478 −4.622 1.00 36.83 O ATOM 774 C SER 95 65.896 12.754 −8.149 1.00 36.83 C ATOM 775 O SER 95 66.184 11.819 −8.883 1.00 36.83 O ATOM 776 N TYR 96 64.785 13.479 −8.280 1.00 36.83 N ATOM 777 CA TYR 96 63.795 13.243 −9.328 1.00 36.83 C ATOM 778 CB TYR 96 62.394 13.139 −8.731 1.00 36.83 C ATOM 779 CG TYR 96 62.328 12.215 −7.552 1.00 36.83 C ATOM 780 CD1 TYR 96 62.848 10.917 −7.618 1.00 36.83 C ATOM 781 CE1 TYR 96 62.806 10.069 −6.506 1.00 36.83 C ATOM 782 CD2 TYR 96 61.765 12.638 −6.354 1.00 36.83 C ATOM 783 CE2 TYR 96 61.714 11.808 −5.251 1.00 36.83 C ATOM 784 CZ TYR 96 62.235 10.531 −5.328 1.00 36.83 C ATOM 785 OH TYR 96 62.181 9.733 −4.211 1.00 36.83 O ATOM 786 C TYR 96 63.808 14.351 −10.378 1.00 36.83 C ATOM 787 O TYR 96 63.759 15.543 −10.062 1.00 36.83 O ATOM 788 N LEU 97 63.863 13.937 −11.634 1.00 36.83 N ATOM 789 CA LEU 97 63.893 14.857 −12.742 1.00 36.83 C ATOM 790 CB LEU 97 65.165 14.601 −13.549 1.00 36.83 C ATOM 791 CG LEU 97 65.882 15.766 −14.241 1.00 36.83 C ATOM 792 CD1 LEU 97 65.766 15.640 −15.764 1.00 36.83 C ATOM 793 CD2 LEU 97 65.330 17.101 −13.733 1.00 36.83 C ATOM 794 C LEU 97 62.649 14.722 −13.623 1.00 36.83 C ATOM 795 O LEU 97 62.622 13.919 −14.563 1.00 36.83 O ATOM 796 N ASN 98 61.611 15.490 −13.301 1.00 36.83 N ATOM 797 CA ASN 98 60.376 15.489 −14.081 1.00 36.83 C ATOM 798 CB ASN 98 59.296 14.579 −13.451 1.00 36.83 C ATOM 799 CG ASN 98 59.029 14.880 −11.978 1.00 36.83 C ATOM 800 OD1 ASN 98 58.576 15.977 −11.608 1.00 36.83 O ATOM 801 ND2 ASN 98 59.297 13.890 −11.124 1.00 36.83 N ATOM 802 C ASN 98 59.877 16.927 −14.222 1.00 36.83 C ATOM 803 O ASN 98 60.319 17.818 −13.492 1.00 36.83 O ATOM 804 N GLU 99 58.963 17.157 −15.161 1.00 36.83 N ATOM 805 CA GLU 99 58.460 18.507 −15.410 1.00 36.83 C ATOM 806 CB GLU 99 57.381 18.470 −16.481 1.00 36.83 C ATOM 807 CG GLU 99 57.946 18.022 −17.818 1.00 36.83 C ATOM 808 CD GLU 99 56.942 18.077 −18.933 1.00 36.83 C ATOM 809 OE1 GLU 99 57.281 17.611 −20.037 1.00 36.83 O ATOM 810 OE2 GLU 99 55.827 18.588 −18.704 1.00 36.83 O ATOM 811 C GLU 99 57.969 19.296 −14.210 1.00 36.83 C ATOM 812 O GLU 99 58.388 20.430 −14.007 1.00 36.83 O ATOM 813 N PRO 100 57.074 18.718 −13.399 1.00 36.83 N ATOM 814 CD PRO 100 56.317 17.458 −13.527 1.00 36.83 C ATOM 815 CA PRO 100 56.613 19.496 −12.247 1.00 36.83 C ATOM 816 CB PRO 100 55.417 18.688 −11.738 1.00 36.83 C ATOM 817 CG PRO 100 55.759 17.284 −12.142 1.00 36.83 C ATOM 818 C PRO 100 57.675 19.727 −11.176 1.00 36.83 C ATOM 819 O PRO 100 57.565 20.670 −10.394 1.00 36.83 O ATOM 820 N ALA 101 58.691 18.870 −11.127 1.00 36.83 N ATOM 821 CA ALA 101 59.751 19.037 −10.140 1.00 36.83 C ATOM 822 CB ALA 101 60.549 17.754 −9.985 1.00 36.83 C ATOM 823 C ALA 101 60.683 20.175 −10.562 1.00 36.83 C ATOM 824 O ALA 101 61.080 21.002 −9.733 1.00 36.83 O ATOM 825 N VAL 102 61.043 20.208 −11.841 1.00 36.83 N ATOM 826 CA VAL 102 61.922 21.253 −12.337 1.00 36.83 C ATOM 827 CB VAL 102 62.403 20.964 −13.783 1.00 36.83 C ATOM 828 CG1 VAL 102 62.946 22.225 −14.429 1.00 36.83 C ATOM 829 CG2 VAL 102 63.509 19.921 −13.751 1.00 36.83 C ATOM 830 C VAL 102 61.214 22.596 −12.270 1.00 36.83 C ATOM 831 O VAL 102 61.829 23.582 −11.898 1.00 36.83 O ATOM 832 N PHE 103 59.924 22.637 −12.604 1.00 36.83 N ATOM 833 CA PHE 103 59.180 23.896 −12.535 1.00 36.83 C ATOM 834 CB PHE 103 57.775 23.745 −13.128 1.00 36.83 C ATOM 835 CG PHE 103 56.887 24.953 −12.917 1.00 36.83 C ATOM 836 CD1 PHE 103 57.253 26.203 −13.395 1.00 36.83 C ATOM 837 CD2 PHE 103 55.683 24.837 −12.239 1.00 36.83 C ATOM 838 CE1 PHE 103 56.439 27.314 −13.205 1.00 36.83 C ATOM 839 CE2 PHE 103 54.858 25.946 −12.041 1.00 36.83 C ATOM 840 CZ PHE 103 55.244 27.187 −12.531 1.00 36.83 C ATOM 841 C PHE 103 59.079 24.382 −11.082 1.00 36.83 C ATOM 842 O PHE 103 59.292 25.561 −10.812 1.00 36.83 O ATOM 843 N HIS 104 58.775 23.476 −10.150 1.00 36.83 N ATOM 844 CA HIS 104 58.658 23.860 −8.741 1.00 36.83 C ATOM 845 CB HIS 104 58.381 22.645 −7.851 1.00 36.83 C ATOM 846 CG HIS 104 58.292 22.978 −6.393 1.00 36.83 C ATOM 847 CD2 HIS 104 59.101 22.658 −5.355 1.00 36.83 C ATOM 848 ND1 HIS 104 57.286 23.758 −5.867 1.00 36.83 N ATOM 849 CE1 HIS 104 57.476 23.905 −4.570 1.00 36.83 C ATOM 850 NE2 HIS 104 58.572 23.248 −4.234 1.00 36.83 N ATOM 851 C HIS 104 59.898 24.581 −8.206 1.00 36.83 C ATOM 852 O HIS 104 59.776 25.631 −7.574 1.00 36.83 O ATOM 853 N ASN 105 61.077 23.998 −8.450 1.00 36.83 N ATOM 854 CA ASN 105 62.346 24.563 −8.001 1.00 36.83 C ATOM 855 CB ASN 105 63.525 23.678 −8.433 1.00 36.83 C ATOM 856 CG ASN 105 64.831 24.063 −7.742 1.00 36.83 C ATOM 857 OD1 ASN 105 64.957 23.942 −6.519 1.00 36.83 O ATOM 858 ND2 ASN 105 65.801 24.531 −8.517 1.00 36.83 N ATOM 859 C ASN 105 62.521 25.968 −8.564 1.00 36.83 C ATOM 860 O ASN 105 62.952 26.859 −7.852 1.00 36.83 O ATOM 861 N LEU 106 62.193 26.155 −9.844 1.00 36.83 N ATOM 862 CA LEU 106 62.285 27.476 −10.466 1.00 36.83 C ATOM 863 CB LEU 106 62.005 27.402 −11.969 1.00 36.83 C ATOM 864 CG LEU 106 63.103 26.829 −12.862 1.00 36.83 C ATOM 865 CD1 LEU 106 62.640 26.876 −14.295 1.00 36.83 C ATOM 866 CD2 LEU 106 64.397 27.630 −12.710 1.00 36.83 C ATOM 867 C LEU 106 61.277 28.421 −9.810 1.00 36.83 C ATOM 868 O LEU 106 61.545 29.611 −9.638 1.00 36.83 O ATOM 869 N ARG 107 60.115 27.881 −9.452 1.00 36.83 N ATOM 870 CA ARG 107 59.067 28.659 −8.801 1.00 36.83 C ATOM 871 CB ARG 107 57.803 27.799 −8.612 1.00 36.83 C ATOM 872 CG ARG 107 56.560 28.539 −8.117 1.00 36.83 C ATOM 873 CD ARG 107 55.595 27.574 −7.402 1.00 36.83 C ATOM 874 NE ARG 107 55.379 26.336 −8.159 1.00 36.83 N ATOM 875 CZ ARG 107 54.986 25.177 −7.621 1.00 36.83 C ATOM 876 NH1 ARG 107 54.761 25.088 −6.316 1.00 36.83 N ATOM 877 NH2 ARG 107 54.833 24.096 −8.383 1.00 36.83 N ATOM 878 C ARG 107 59.597 29.123 −7.442 1.00 36.83 C ATOM 879 O ARG 107 59.485 30.300 −7.093 1.00 36.83 O ATOM 880 N VAL 108 60.183 28.196 −6.684 1.00 36.83 N ATOM 881 CA VAL 108 60.723 28.518 −5.364 1.00 36.83 C ATOM 882 CB VAL 108 61.363 27.277 −4.689 1.00 36.83 C ATOM 883 CG1 VAL 108 62.029 27.682 −3.381 1.00 36.83 C ATOM 884 CG2 VAL 108 60.304 26.229 −4.405 1.00 36.83 C ATOM 885 C VAL 108 61.772 29.624 −5.433 1.00 36.83 C ATOM 886 O VAL 108 61.765 30.558 −4.636 1.00 36.83 O ATOM 887 N ARG 109 62.677 29.521 −6.388 1.00 36.83 N ATOM 888 CA ARG 109 63.713 30.533 −6.518 1.00 36.83 C ATOM 889 CB ARG 109 64.823 30.023 −7.452 1.00 36.83 C ATOM 890 CG ARG 109 65.545 28.783 −6.893 1.00 36.83 C ATOM 891 CD ARG 109 66.640 28.268 −7.824 1.00 36.83 C ATOM 892 NE ARG 109 67.650 29.288 −8.094 1.00 36.83 N ATOM 893 CZ ARG 109 68.484 29.775 −7.177 1.00 36.83 C ATOM 894 NH1 ARG 109 68.443 29.337 −5.921 1.00 36.83 N ATOM 895 NH2 ARG 109 69.357 30.710 −7.513 1.00 36.83 N ATOM 896 C ARG 109 63.127 31.863 −6.993 1.00 36.83 C ATOM 897 O ARG 109 63.443 32.916 −6.451 1.00 36.83 O ATOM 898 N TYR 110 62.237 31.804 −7.977 1.00 36.83 N ATOM 899 CA TYR 110 61.597 32.997 −8.525 1.00 36.83 C ATOM 900 CB TYR 110 60.685 32.616 −9.695 1.00 36.83 C ATOM 901 CG TYR 110 60.200 33.786 −10.530 1.00 36.83 C ATOM 902 CD1 TYR 110 61.045 34.418 −11.445 1.00 36.83 C ATOM 903 CE1 TYR 110 60.603 35.471 −12.228 1.00 36.83 C ATOM 904 CD2 TYR 110 58.892 34.249 −10.421 1.00 36.83 C ATOM 905 CE2 TYR 110 58.435 35.312 −11.208 1.00 36.83 C ATOM 906 CZ TYR 110 59.294 35.913 −12.105 1.00 36.83 C ATOM 907 OH TYR 110 58.846 36.954 −12.881 1.00 36.83 O ATOM 908 C TYR 110 60.779 33.714 −7.451 1.00 36.83 C ATOM 909 O TYR 110 60.729 34.943 −7.423 1.00 36.83 O ATOM 910 N ASN 111 60.140 32.940 −6.574 1.00 36.83 N ATOM 911 CA ASN 111 59.309 33.503 −5.509 1.00 36.83 C ATOM 912 CB ASN 111 58.598 32.395 −4.739 1.00 36.83 C ATOM 913 CG ASN 111 57.522 31.711 −5.568 1.00 36.83 C ATOM 914 OD1 ASN 111 56.714 32.370 −6.222 1.00 36.83 O ATOM 915 ND2 ASN 111 57.503 30.385 −5.536 1.00 36.83 N ATOM 916 C ASN 111 60.076 34.389 −4.541 1.00 36.83 C ATOM 917 O ASN 111 59.479 35.188 −3.838 1.00 36.83 O ATOM 918 N GLN 112 61.394 34.226 −4.469 1.00 36.83 N ATOM 919 CA GLN 112 62.176 35.099 −3.617 1.00 36.83 C ATOM 920 CB GLN 112 62.776 34.339 −2.404 1.00 36.83 C ATOM 921 CG GLN 112 63.784 33.225 −2.648 1.00 36.83 C ATOM 922 CD GLN 112 64.309 32.634 −1.321 1.00 36.83 C ATOM 923 OE1 GLN 112 63.567 32.011 −0.561 1.00 36.83 O ATOM 924 NE2 GLN 112 65.585 32.848 −1.043 1.00 36.83 N ATOM 925 C GLN 112 63.233 35.802 −4.497 1.00 36.83 C ATOM 926 O GLN 112 64.411 35.933 −4.157 1.00 36.83 O ATOM 927 N ASP 113 62.742 36.239 −5.657 1.00 36.83 N ATOM 928 CA ASP 113 63.506 36.948 −6.681 1.00 36.83 C ATOM 929 CB ASP 113 63.696 38.408 −6.273 1.00 36.83 C ATOM 930 CG ASP 113 62.381 39.143 −6.150 1.00 36.83 C ATOM 931 OD1 ASP 113 61.424 38.782 −6.880 1.00 36.83 O ATOM 932 OD2 ASP 113 62.303 40.080 −5.328 1.00 36.83 O ATOM 933 C ASP 113 64.841 36.379 −7.143 1.00 36.83 C ATOM 934 O ASP 113 65.732 37.132 −7.526 1.00 36.83 O ATOM 935 N LEU 114 64.989 35.060 −7.113 1.00 36.83 N ATOM 936 CA LEU 114 66.218 34.442 −7.597 1.00 36.83 C ATOM 937 CB LEU 114 66.569 33.216 −6.767 1.00 36.83 C ATOM 938 CG LEU 114 66.912 33.403 −5.285 1.00 36.83 C ATOM 939 CD1 LEU 114 67.328 32.039 −4.730 1.00 36.83 C ATOM 940 CD2 LEU 114 68.040 34.431 −5.087 1.00 36.83 C ATOM 941 C LEU 114 65.897 34.028 −9.039 1.00 36.83 C ATOM 942 O LEU 114 65.242 33.019 −9.261 1.00 36.83 O ATOM 943 N ILE 115 66.354 34.808 −10.015 1.00 36.83 N ATOM 944 CA ILE 115 66.045 34.507 −11.407 1.00 36.83 C ATOM 945 CB ILE 115 65.921 35.798 −12.227 1.00 36.83 C ATOM 946 CG2 ILE 115 64.885 36.709 −11.575 1.00 36.83 C ATOM 947 CG1 ILE 115 67.274 36.506 −12.314 1.00 36.83 C ATOM 948 CD1 ILE 115 67.230 37.808 −13.079 1.00 36.83 C ATOM 949 C ILE 115 66.973 33.548 −12.131 1.00 36.83 C ATOM 950 O ILE 115 66.577 32.933 −13.124 1.00 36.83 O ATOM 951 N TYR 116 68.202 33.414 −11.650 1.00 36.83 N ATOM 952 CA TYR 116 69.144 32.506 −12.282 1.00 36.83 C ATOM 953 CB TYR 116 70.541 33.132 −12.322 1.00 36.83 C ATOM 954 CG TYR 116 70.612 34.389 −13.157 1.00 36.83 C ATOM 955 CD1 TYR 116 70.478 34.337 −14.546 1.00 36.83 C ATOM 956 CE1 TYR 116 70.501 35.508 −15.317 1.00 36.83 C ATOM 957 CD2 TYR 116 70.775 35.636 −12.558 1.00 36.83 C ATOM 958 CE2 TYR 116 70.799 36.801 −13.313 1.00 36.83 C ATOM 959 CZ TYR 116 70.657 36.733 −14.695 1.00 36.83 C ATOM 960 OH TYR 116 70.635 37.889 −15.439 1.00 36.83 O ATOM 961 C TYR 116 69.193 31.154 −11.567 1.00 36.83 C ATOM 962 O TYR 116 69.184 31.081 −10.335 1.00 36.83 O ATOM 963 N THR 117 69.224 30.091 −12.368 1.00 36.83 N ATOM 964 CA THR 117 69.293 28.708 −11.898 1.00 36.83 C ATOM 965 CB THR 117 67.900 28.104 −11.680 1.00 36.83 C ATOM 966 OG1 THR 117 67.087 29.010 −10.925 1.00 36.83 O ATOM 967 CG2 THR 117 68.016 26.787 −10.911 1.00 36.83 C ATOM 968 C THR 117 69.992 27.874 −12.986 1.00 36.83 C ATOM 969 O THR 117 69.705 28.035 −14.168 1.00 36.83 O ATOM 970 N TYR 118 70.917 27.005 −12.594 1.00 36.83 N ATOM 971 CA TYR 118 71.605 26.157 −13.560 1.00 36.83 C ATOM 972 CB TYR 118 73.026 25.816 −13.104 1.00 36.83 C ATOM 973 CG TYR 118 73.973 26.979 −13.045 1.00 36.83 C ATOM 974 CD1 TYR 118 74.282 27.710 −14.188 1.00 36.83 C ATOM 975 CE1 TYR 118 75.160 28.784 −14.127 1.00 36.83 C ATOM 976 CD2 TYR 118 74.566 27.354 −11.836 1.00 36.83 C ATOM 977 CE2 TYR 118 75.435 28.424 −11.767 1.00 36.83 C ATOM 978 CZ TYR 118 75.732 29.135 −12.910 1.00 36.83 C ATOM 979 OH TYR 118 76.613 30.189 −12.840 1.00 36.83 O ATOM 980 C TYR 118 70.862 24.842 −13.775 1.00 36.83 C ATOM 981 O TYR 118 70.203 24.328 −12.879 1.00 36.83 O ATOM 982 N SER 119 70.990 24.313 −14.983 1.00 36.83 N ATOM 983 CA SER 119 70.389 23.043 −15.366 1.00 36.83 C ATOM 984 CB SER 119 69.391 23.221 −16.506 1.00 36.83 C ATOM 985 OG SER 119 68.342 24.093 −16.132 1.00 36.83 O ATOM 986 C SER 119 71.557 22.221 −15.858 1.00 36.83 C ATOM 987 O SER 119 71.471 21.557 −16.890 1.00 36.83 O ATOM 988 N GLY 120 72.651 22.272 −15.106 1.00 36.83 N ATOM 989 CA GLY 120 73.842 21.558 −15.496 1.00 36.83 C ATOM 990 C GLY 120 74.817 22.531 −16.133 1.00 36.83 C ATOM 991 O GLY 120 75.213 23.524 −15.515 1.00 36.83 O ATOM 992 N LEU 121 75.198 22.259 −17.376 1.00 36.83 N ATOM 993 CA LEU 121 76.142 23.105 −18.085 1.00 36.83 C ATOM 994 CB LEU 121 76.835 22.295 −19.187 1.00 36.83 C ATOM 995 CG LEU 121 78.066 21.507 −18.706 1.00 36.83 C ATOM 996 CD1 LEU 121 78.623 20.668 −19.852 1.00 36.83 C ATOM 997 CD2 LEU 121 79.133 22.479 −18.184 1.00 36.83 C ATOM 998 C LEU 121 75.614 24.424 −18.663 1.00 36.83 C ATOM 999 O LEU 121 76.413 25.262 −19.085 1.00 36.83 O ATOM 1000 N PHE 122 74.295 24.616 −18.703 1.00 36.83 N ATOM 1001 CA PHE 122 73.744 25.877 −19.204 1.00 36.83 C ATOM 1002 CB PHE 122 72.883 25.675 −20.460 1.00 36.83 C ATOM 1003 CG PHE 122 71.812 24.626 −20.318 1.00 36.83 C ATOM 1004 CD1 PHE 122 72.065 23.303 −20.666 1.00 36.83 C ATOM 1005 CD2 PHE 122 70.544 24.964 −19.855 1.00 36.83 C ATOM 1006 CE1 PHE 122 71.068 22.337 −20.557 1.00 36.83 C ATOM 1007 CE2 PHE 122 69.533 23.996 −19.743 1.00 36.83 C ATOM 1008 CZ PHE 122 69.798 22.686 −20.095 1.00 36.83 C ATOM 1009 C PHE 122 72.927 26.574 −18.116 1.00 36.83 C ATOM 1010 O PHE 122 72.455 25.931 −17.184 1.00 36.83 O ATOM 1011 N LEU 123 72.769 27.889 −18.245 1.00 36.83 N ATOM 1012 CA LEU 123 72.043 28.698 −17.272 1.00 36.83 C ATOM 1013 CB LEU 123 72.787 30.028 −17.095 1.00 36.83 C ATOM 1014 CG LEU 123 72.194 31.084 −16.162 1.00 36.83 C ATOM 1015 CD1 LEU 123 72.138 30.560 −14.724 1.00 36.83 C ATOM 1016 CD2 LEU 123 73.052 32.349 −16.243 1.00 36.83 C ATOM 1017 C LEU 123 70.587 28.980 −17.668 1.00 36.83 C ATOM 1018 O LEU 123 70.292 29.127 −18.840 1.00 36.83 O ATOM 1019 N VAL 124 69.683 29.059 −16.697 1.00 36.83 N ATOM 1020 CA VAL 124 68.275 29.367 −16.988 1.00 36.83 C ATOM 1021 CB VAL 124 67.302 28.265 −16.446 1.00 36.83 C ATOM 1022 CG1 VAL 124 65.856 28.743 −16.523 1.00 36.83 C ATOM 1023 CG2 VAL 124 67.464 26.973 −17.260 1.00 36.83 C ATOM 1024 C VAL 124 67.965 30.706 −16.330 1.00 36.83 C ATOM 1025 O VAL 124 68.350 30.945 −15.184 1.00 36.83 O ATOM 1026 N ALA 125 67.280 31.580 −17.055 1.00 36.83 N ATOM 1027 CA ALA 125 66.947 32.912 −16.552 1.00 36.83 C ATOM 1028 CB ALA 125 67.766 33.943 −17.289 1.00 36.83 C ATOM 1029 C ALA 125 65.466 33.221 −16.729 1.00 36.83 C ATOM 1030 O ALA 125 64.980 33.241 −17.845 1.00 36.83 O ATOM 1031 N VAL 126 64.757 33.477 −15.633 1.00 36.83 N ATOM 1032 CA VAL 126 63.326 33.770 −15.706 1.00 36.83 C ATOM 1033 CB VAL 126 62.524 32.934 −14.661 1.00 36.83 C ATOM 1034 CG1 VAL 126 61.031 33.108 −14.883 1.00 36.83 C ATOM 1035 CG2 VAL 126 62.905 31.458 −14.760 1.00 36.83 C ATOM 1036 C VAL 126 63.090 35.263 −15.477 1.00 36.83 C ATOM 1037 O VAL 126 63.373 35.793 −14.399 1.00 36.83 O ATOM 1038 N ASN 127 62.576 35.929 −16.505 1.00 36.83 N ATOM 1039 CA ASN 127 62.326 37.372 −16.471 1.00 36.83 C ATOM 1040 CB ASN 127 61.567 37.815 −17.730 1.00 36.83 C ATOM 1041 CG ASN 127 61.635 39.326 −17.958 1.00 36.83 C ATOM 1042 OD1 ASN 127 61.703 40.108 −17.009 1.00 36.83 O ATOM 1043 ND2 ASN 127 61.602 39.734 −19.215 1.00 36.83 N ATOM 1044 C ASN 127 61.565 37.863 −15.245 1.00 36.83 C ATOM 1045 O ASN 127 60.409 37.494 −15.024 1.00 36.83 O ATOM 1046 N PRO 128 62.204 38.720 −14.436 1.00 36.83 N ATOM 1047 CD PRO 128 63.605 39.176 −14.516 1.00 36.83 C ATOM 1048 CA PRO 128 61.548 39.247 −13.241 1.00 36.83 C ATOM 1049 CB PRO 128 62.716 39.821 −12.435 1.00 36.83 C ATOM 1050 CG PRO 128 63.644 40.320 −13.520 1.00 36.83 C ATOM 1051 C PRO 128 60.489 40.306 −13.561 1.00 36.83 C ATOM 1052 O PRO 128 59.469 40.382 −12.895 1.00 36.83 O ATOM 1053 N PHE 129 60.725 41.109 −14.594 1.00 36.83 N ATOM 1054 CA PHE 129 59.789 42.180 −14.947 1.00 36.83 C ATOM 1055 CB PHE 129 58.397 41.641 −15.280 1.00 36.83 C ATOM 1056 CG PHE 129 58.248 41.220 −16.707 1.00 36.83 C ATOM 1057 CD1 PHE 129 58.568 42.099 −17.738 1.00 36.83 C ATOM 1058 CD2 PHE 129 57.828 39.937 −17.026 1.00 36.83 C ATOM 1059 CE1 PHE 129 58.477 41.701 −19.076 1.00 36.83 C ATOM 1060 CE2 PHE 129 57.734 39.531 −18.345 1.00 36.83 C ATOM 1061 CZ PHE 129 58.061 40.414 −19.380 1.00 36.83 C ATOM 1062 C PHE 129 59.707 43.130 −13.774 1.00 36.83 C ATOM 1063 O PHE 129 58.644 43.621 −13.415 1.00 36.83 O ATOM 1064 N LYS 130 60.861 43.350 −13.166 1.00 36.83 N ATOM 1065 CA LYS 130 61.009 44.249 −12.036 1.00 36.83 C ATOM 1066 CB LYS 130 60.292 43.703 −10.790 1.00 36.83 C ATOM 1067 CG LYS 130 61.175 43.183 −9.664 1.00 36.83 C ATOM 1068 CD LYS 130 60.309 42.951 −8.415 1.00 36.83 C ATOM 1069 CE LYS 130 61.023 42.190 −7.300 1.00 36.83 C ATOM 1070 NZ LYS 130 60.123 42.008 −6.119 1.00 36.83 N ATOM 1071 C LYS 130 62.498 44.335 −11.803 1.00 36.83 C ATOM 1072 O LYS 130 63.224 43.393 −12.097 1.00 36.83 O ATOM 1073 N ILE 131 62.955 45.469 −11.295 1.00 36.83 N ATOM 1074 CA ILE 131 64.370 45.644 −11.054 1.00 36.83 C ATOM 1075 CB ILE 131 64.712 47.133 −10.876 1.00 36.83 C ATOM 1076 CG2 ILE 131 66.120 47.265 −10.359 1.00 36.83 C ATOM 1077 CG1 ILE 131 64.539 47.872 −12.209 1.00 36.83 C ATOM 1078 CD1 ILE 131 64.602 49.391 −12.104 1.00 36.83 C ATOM 1079 C ILE 131 64.823 44.881 −9.820 1.00 36.83 C ATOM 1080 O ILE 131 64.083 44.751 −8.846 1.00 36.83 O ATOM 1081 N ILE 132 66.048 44.376 −9.879 1.00 36.83 N ATOM 1082 CA ILE 132 66.631 43.639 −8.778 1.00 36.83 C ATOM 1083 CB ILE 132 66.496 42.127 −9.004 1.00 36.83 C ATOM 1084 CG2 ILE 132 67.270 41.373 −7.940 1.00 36.83 C ATOM 1085 CG1 ILE 132 65.010 41.737 −9.005 1.00 36.83 C ATOM 1086 CD1 ILE 132 64.759 40.285 −9.379 1.00 36.83 C ATOM 1087 C ILE 132 68.109 44.027 −8.692 1.00 36.83 C ATOM 1088 O ILE 132 68.835 43.951 −9.681 1.00 36.83 O ATOM 1089 N PRO 133 68.569 44.437 −7.493 1.00 36.83 N ATOM 1090 CD PRO 133 67.681 44.505 −6.317 1.00 36.83 C ATOM 1091 CA PRO 133 69.928 44.875 −7.126 1.00 36.83 C ATOM 1092 CB PRO 133 69.793 45.218 −5.640 1.00 36.83 C ATOM 1093 CG PRO 133 68.362 45.543 −5.473 1.00 36.83 C ATOM 1094 C PRO 133 71.117 43.936 −7.341 1.00 36.83 C ATOM 1095 O PRO 133 72.000 43.894 −6.493 1.00 36.83 O ATOM 1096 N ILE 134 71.193 43.204 −8.447 1.00 36.83 N ATOM 1097 CA ILE 134 72.343 42.312 −8.595 1.00 36.83 C ATOM 1098 CB ILE 134 71.885 40.837 −8.735 1.00 36.83 C ATOM 1099 CG2 ILE 134 71.073 40.450 −7.528 1.00 36.83 C ATOM 1100 CG1 ILE 134 71.070 40.653 −10.022 1.00 36.83 C ATOM 1101 CD1 ILE 134 70.596 39.230 −10.276 1.00 36.83 C ATOM 1102 C ILE 134 73.309 42.633 −9.727 1.00 36.83 C ATOM 1103 O ILE 134 74.186 41.829 −10.043 1.00 36.83 O ATOM 1104 N TYR 135 73.188 43.812 −10.321 1.00 36.83 N ATOM 1105 CA TYR 135 74.065 44.157 −11.433 1.00 36.83 C ATOM 1106 CB TYR 135 73.221 44.385 −12.693 1.00 36.83 C ATOM 1107 CG TYR 135 72.284 43.240 −13.029 1.00 36.83 C ATOM 1108 CD1 TYR 135 72.774 42.027 −13.494 1.00 36.83 C ATOM 1109 CE1 TYR 135 71.905 40.975 −13.829 1.00 36.83 C ATOM 1110 CD2 TYR 135 70.900 43.386 −12.898 1.00 36.83 C ATOM 1111 CE2 TYR 135 70.024 42.348 −13.230 1.00 36.83 C ATOM 1112 CZ TYR 135 70.534 41.150 −13.696 1.00 36.83 C ATOM 1113 OH TYR 135 69.678 40.135 −14.036 1.00 36.83 O ATOM 1114 C TYR 135 74.953 45.377 −11.173 1.00 36.83 C ATOM 1115 O TYR 135 75.142 46.211 −12.056 1.00 36.83 O ATOM 1116 N THR 136 75.493 45.474 −9.959 1.00 36.83 N ATOM 1117 CA THR 136 76.356 46.589 −9.588 1.00 36.83 C ATOM 1118 CB THR 136 76.101 47.023 −8.138 1.00 36.83 C ATOM 1119 OG1 THR 136 76.396 45.937 −7.257 1.00 36.83 O ATOM 1120 CG2 THR 136 74.659 47.437 −7.952 1.00 36.83 C ATOM 1121 C THR 136 77.825 46.197 −9.710 1.00 36.83 C ATOM 1122 O THR 136 78.148 45.028 −9.991 1.00 36.83 O ATOM 1123 N GLN 137 78.717 47.165 −9.490 1.00 36.83 N ATOM 1124 CA GLN 137 80.156 46.893 −9.560 1.00 36.83 C ATOM 1125 CB GLN 137 80.989 48.176 −9.423 1.00 36.83 C ATOM 1126 CG GLN 137 81.600 48.676 −10.728 1.00 36.83 C ATOM 1127 CD GLN 137 82.341 47.595 −11.512 1.00 36.83 C ATOM 1128 OE1 GLN 137 83.181 46.870 −10.977 1.00 36.83 O ATOM 1129 NE2 GLN 137 82.034 47.498 −12.792 1.00 36.83 N ATOM 1130 C GLN 137 80.543 45.933 −8.450 1.00 36.83 C ATOM 1131 O GLN 137 81.429 45.086 −8.629 1.00 36.83 O ATOM 1132 N GLU 138 79.886 46.053 −7.303 1.00 36.83 N ATOM 1133 CA GLU 138 80.190 45.151 −6.199 1.00 36.83 C ATOM 1134 CB GLU 138 79.427 45.544 −4.931 1.00 36.83 C ATOM 1135 CG GLU 138 79.983 46.766 −4.206 1.00 36.83 C ATOM 1136 CD GLU 138 79.915 48.014 −5.061 1.00 36.83 C ATOM 1137 OE1 GLU 138 78.816 48.295 −5.618 1.00 36.83 O ATOM 1138 OE2 GLU 138 80.960 48.708 −5.180 1.00 36.83 O ATOM 1139 C GLU 138 79.839 43.719 −6.577 1.00 36.83 C ATOM 1140 O GLU 138 80.511 42.785 −6.160 1.00 36.83 O ATOM 1141 N MET 139 78.781 43.535 −7.356 1.00 36.83 N ATOM 1142 CA MET 139 78.412 42.185 −7.761 1.00 36.83 C ATOM 1143 CB MET 139 77.029 42.184 −8.410 1.00 36.83 C ATOM 1144 CG MET 139 75.885 42.439 −7.405 1.00 36.83 C ATOM 1145 SD MET 139 75.810 41.167 −6.118 1.00 36.83 S ATOM 1146 CE MET 139 74.556 41.783 −5.059 1.00 36.83 C ATOM 1147 C MET 139 79.476 41.639 −8.710 1.00 36.83 C ATOM 1148 O MET 139 79.948 40.509 −8.552 1.00 36.83 O ATOM 1149 N VAL 140 79.865 42.454 −9.682 1.00 36.83 N ATOM 1150 CA VAL 140 80.894 42.075 −10.635 1.00 36.83 C ATOM 1151 CB VAL 140 81.254 43.256 −11.560 1.00 36.83 C ATOM 1152 CG1 VAL 140 82.410 42.869 −12.486 1.00 36.83 C ATOM 1153 CG2 VAL 140 80.023 43.678 −12.378 1.00 36.83 C ATOM 1154 C VAL 140 82.167 41.615 −9.915 1.00 36.83 C ATOM 1155 O VAL 140 82.705 40.544 −10.209 1.00 36.83 O ATOM 1156 N ASP 141 82.643 42.421 −8.973 1.00 36.83 N ATOM 1157 CA ASP 141 83.859 42.095 −8.228 1.00 36.83 C ATOM 1158 CB ASP 141 84.157 43.188 −7.211 1.00 36.83 C ATOM 1159 CG ASP 141 84.544 44.491 −7.865 1.00 36.83 C ATOM 1160 OD1 ASP 141 84.623 45.503 −7.132 1.00 36.83 O ATOM 1161 OD2 ASP 141 84.769 44.498 −9.105 1.00 36.83 O ATOM 1162 C ASP 141 83.752 40.756 −7.509 1.00 36.83 C ATOM 1163 O ASP 141 84.730 40.008 −7.398 1.00 36.83 O ATOM 1164 N ILE 142 82.560 40.467 −7.009 1.00 36.83 N ATOM 1165 CA ILE 142 82.331 39.212 −6.324 1.00 36.83 C ATOM 1166 CB ILE 142 80.903 39.146 −5.743 1.00 36.83 C ATOM 1167 CG2 ILE 142 80.571 37.722 −5.320 1.00 36.83 C ATOM 1168 CG1 ILE 142 80.777 40.120 −4.568 1.00 36.83 C ATOM 1169 CD1 ILE 142 81.798 39.875 −3.462 1.00 36.83 C ATOM 1170 C ILE 142 82.528 38.020 −7.263 1.00 36.83 C ATOM 1171 O ILE 142 83.073 37.002 −6.846 1.00 36.83 O ATOM 1172 N PHE 143 82.102 38.143 −8.518 1.00 36.83 N ATOM 1173 CA PHE 143 82.219 37.025 −9.461 1.00 36.83 C ATOM 1174 CB PHE 143 81.080 37.062 −10.496 1.00 36.83 C ATOM 1175 CG PHE 143 79.736 36.749 −9.928 1.00 36.83 C ATOM 1176 CD1 PHE 143 79.013 37.716 −9.245 1.00 36.83 C ATOM 1177 CD2 PHE 143 79.200 35.474 −10.048 1.00 36.83 C ATOM 1178 CE1 PHE 143 77.772 37.413 −8.686 1.00 36.83 C ATOM 1179 CE2 PHE 143 77.980 35.171 −9.501 1.00 36.83 C ATOM 1180 CZ PHE 143 77.262 36.140 −8.817 1.00 36.83 C ATOM 1181 C PHE 143 83.541 36.907 −10.200 1.00 36.83 C ATOM 1182 O PHE 143 83.835 35.861 −10.785 1.00 36.83 O ATOM 1183 N LYS 144 84.327 37.980 −10.173 1.00 36.83 N ATOM 1184 CA LYS 144 85.618 38.007 −10.843 1.00 36.83 C ATOM 1185 CB LYS 144 86.409 39.250 −10.406 1.00 36.83 C ATOM 1186 CG LYS 144 87.676 39.568 −11.225 1.00 36.83 C ATOM 1187 CD LYS 144 88.776 38.517 −11.065 1.00 36.83 C ATOM 1188 CE LYS 144 89.229 38.362 −9.604 1.00 36.83 C ATOM 1189 NZ LYS 144 90.136 37.186 −9.386 1.00 36.83 N ATOM 1190 C LYS 144 86.386 36.744 −10.494 1.00 36.83 C ATOM 1191 O LYS 144 86.645 36.463 −9.323 1.00 36.83 O ATOM 1192 N GLY 145 86.724 35.966 −11.517 1.00 36.83 N ATOM 1193 CA GLY 145 87.482 34.739 −11.309 1.00 36.83 C ATOM 1194 C GLY 145 86.935 33.632 −10.424 1.00 36.83 C ATOM 1195 O GLY 145 87.684 32.715 −10.074 1.00 36.83 O ATOM 1196 N ARG 146 85.659 33.678 −10.055 1.00 36.83 N ATOM 1197 CA ARG 146 85.098 32.620 −9.207 1.00 36.83 C ATOM 1198 CB ARG 146 83.874 33.128 −8.441 1.00 36.83 C ATOM 1199 CG ARG 146 84.149 34.018 −7.236 1.00 36.83 C ATOM 1200 CD ARG 146 85.027 33.318 −6.200 1.00 36.83 C ATOM 1201 NE ARG 146 86.410 33.766 −6.318 1.00 36.83 N ATOM 1202 CZ ARG 146 86.825 34.967 −5.925 1.00 36.83 C ATOM 1203 NH1 ARG 146 85.955 35.816 −5.377 1.00 36.83 N ATOM 1204 NH2 ARG 146 88.092 35.334 −6.117 1.00 36.83 N ATOM 1205 C ARG 146 84.689 31.397 −10.038 1.00 36.83 C ATOM 1206 O ARG 146 84.113 31.539 −11.118 1.00 36.83 O ATOM 1207 N ARG 147 84.984 30.193 −9.548 1.00 36.83 N ATOM 1208 CA ARG 147 84.598 28.986 −10.279 1.00 36.83 C ATOM 1209 CB ARG 147 85.231 27.735 −9.656 1.00 36.83 C ATOM 1210 CG ARG 147 86.762 27.717 −9.583 1.00 36.83 C ATOM 1211 CD ARG 147 87.417 27.646 −10.951 1.00 36.83 C ATOM 1212 NE ARG 147 86.764 26.668 −11.816 1.00 36.83 N ATOM 1213 CZ ARG 147 87.401 25.941 −12.735 1.00 36.83 C ATOM 1214 NH1 ARG 147 88.712 26.081 −12.900 1.00 36.83 N ATOM 1215 NH2 ARG 147 86.726 25.079 −13.495 1.00 36.83 N ATOM 1216 C ARG 147 83.071 28.869 −10.181 1.00 36.83 C ATOM 1217 O ARG 147 82.489 29.144 −9.134 1.00 36.83 O ATOM 1218 N ARG 148 82.425 28.442 −11.259 1.00 36.83 N ATOM 1219 CA ARG 148 80.972 28.319 −11.261 1.00 36.83 C ATOM 1220 CB ARG 148 80.507 27.517 −12.473 1.00 36.83 C ATOM 1221 CG ARG 148 79.456 28.212 −13.310 1.00 36.83 C ATOM 1222 CD ARG 148 78.823 27.214 −14.259 1.00 36.83 C ATOM 1223 NE ARG 148 78.097 26.180 −13.522 1.00 36.83 N ATOM 1224 CZ ARG 148 77.258 25.314 −14.081 1.00 36.83 C ATOM 1225 NH1 ARG 148 77.036 25.349 −15.388 1.00 36.83 N ATOM 1226 NH2 ARG 148 76.635 24.419 −13.323 1.00 36.83 N ATOM 1227 C ARG 148 80.369 27.700 −10.001 1.00 36.83 C ATOM 1228 O ARG 148 79.442 28.260 −9.433 1.00 36.83 O ATOM 1229 N ASN 149 80.876 26.553 −9.553 1.00 36.83 N ATOM 1230 CA ASN 149 80.302 25.926 −8.357 1.00 36.83 C ATOM 1231 CB ASN 149 80.532 24.401 −8.360 1.00 36.83 C ATOM 1232 CG ASN 149 81.960 24.000 −8.012 1.00 36.83 C ATOM 1233 OD1 ASN 149 82.417 24.193 −6.885 1.00 36.83 O ATOM 1234 ND2 ASN 149 82.665 23.423 −8.979 1.00 36.83 N ATOM 1235 C ASN 149 80.765 26.523 −7.040 1.00 36.83 C ATOM 1236 O ASN 149 80.580 25.910 −5.987 1.00 36.83 O ATOM 1237 N GLU 150 81.354 27.720 −7.095 1.00 36.83 N ATOM 1238 CA GLU 150 81.829 28.416 −5.892 1.00 36.83 C ATOM 1239 CB GLU 150 83.302 28.824 −6.058 1.00 36.83 C ATOM 1240 CG GLU 150 84.272 27.664 −5.776 1.00 36.83 C ATOM 1241 CD GLU 150 85.695 28.116 −5.471 1.00 36.83 C ATOM 1242 OE1 GLU 150 86.427 27.356 −4.775 1.00 36.83 O ATOM 1243 OE2 GLU 150 86.079 29.222 −5.931 1.00 36.83 O ATOM 1244 C GLU 150 80.962 29.643 −5.537 1.00 36.83 C ATOM 1245 O GLU 150 80.968 30.104 −4.394 1.00 36.83 O ATOM 1246 N VAL 151 80.229 30.168 −6.519 1.00 36.83 N ATOM 1247 CA VAL 151 79.324 31.303 −6.304 1.00 36.83 C ATOM 1248 CB VAL 151 79.788 32.570 −7.055 1.00 36.83 C ATOM 1249 CG1 VAL 151 81.086 33.064 −6.479 1.00 36.83 C ATOM 1250 CG2 VAL 151 79.942 32.268 −8.539 1.00 36.83 C ATOM 1251 C VAL 151 77.932 30.930 −6.829 1.00 36.83 C ATOM 1252 O VAL 151 77.773 29.920 −7.513 1.00 36.83 O ATOM 1253 N ALA 152 76.936 31.759 −6.528 1.00 36.83 N ATOM 1254 CA ALA 152 75.566 31.500 −6.978 1.00 36.83 C ATOM 1255 CB ALA 152 74.597 32.429 −6.265 1.00 36.83 C ATOM 1256 C ALA 152 75.409 31.669 −8.481 1.00 36.83 C ATOM 1257 O ALA 152 76.248 32.287 −9.139 1.00 36.83 O ATOM 1258 N PRO 153 74.326 31.112 −9.047 1.00 36.83 N ATOM 1259 CD PRO 153 73.388 30.157 −8.427 1.00 36.83 C ATOM 1260 CA PRO 153 74.078 31.229 −10.484 1.00 36.83 C ATOM 1261 CB PRO 153 72.802 30.414 −10.682 1.00 36.83 C ATOM 1262 CG PRO 153 72.915 29.351 −9.620 1.00 36.83 C ATOM 1263 C PRO 153 73.884 32.704 −10.838 1.00 36.83 C ATOM 1264 O PRO 153 73.189 33.434 −10.125 1.00 36.83 O ATOM 1265 N HIS 154 74.499 33.139 −11.932 1.00 36.83 N ATOM 1266 CA HIS 154 74.389 34.524 −12.356 1.00 36.83 C ATOM 1267 CB HIS 154 75.233 35.407 −11.423 1.00 36.83 C ATOM 1268 CG HIS 154 74.908 36.868 −11.497 1.00 36.83 C ATOM 1269 CD2 HIS 154 74.310 37.693 −10.605 1.00 36.83 C ATOM 1270 ND1 HIS 154 75.183 37.640 −12.605 1.00 36.83 N ATOM 1271 CE1 HIS 154 74.764 38.874 −12.394 1.00 36.83 C ATOM 1272 NE2 HIS 154 74.232 38.934 −11.189 1.00 36.83 N ATOM 1273 C HIS 154 74.882 34.650 −13.797 1.00 36.83 C ATOM 1274 O HIS 154 75.678 33.823 −14.259 1.00 36.83 O ATOM 1275 N ILE 155 74.400 35.667 −14.510 1.00 36.83 N ATOM 1276 CA ILE 155 74.838 35.889 −15.880 1.00 36.83 C ATOM 1277 CB ILE 155 73.975 36.971 −16.614 1.00 36.83 C ATOM 1278 CG2 ILE 155 74.039 38.280 −15.882 1.00 36.83 C ATOM 1279 CG1 ILE 155 74.473 37.181 −18.054 1.00 36.83 C ATOM 1280 CD1 ILE 155 74.409 35.935 −18.942 1.00 36.83 C ATOM 1281 C ILE 155 76.300 36.325 −15.849 1.00 36.83 C ATOM 1282 O ILE 155 76.981 36.265 −16.863 1.00 36.83 O ATOM 1283 N PHE 156 76.783 36.749 −14.682 1.00 36.83 N ATOM 1284 CA PHE 156 78.183 37.183 −14.529 1.00 36.83 C ATOM 1285 CB PHE 156 78.374 38.053 −13.277 1.00 36.83 C ATOM 1286 CG PHE 156 77.835 39.461 −13.401 1.00 36.83 C ATOM 1287 CD1 PHE 156 77.562 40.021 −14.641 1.00 36.83 C ATOM 1288 CD2 PHE 156 77.636 40.235 −12.262 1.00 36.83 C ATOM 1289 CE1 PHE 156 77.100 41.330 −14.747 1.00 36.83 C ATOM 1290 CE2 PHE 156 77.172 41.547 −12.359 1.00 36.83 C ATOM 1291 CZ PHE 156 76.903 42.095 −13.606 1.00 36.83 C ATOM 1292 C PHE 156 79.102 35.979 −14.415 1.00 36.83 C ATOM 1293 O PHE 156 80.221 35.996 −14.915 1.00 36.83 O ATOM 1294 N ALA 157 78.622 34.938 −13.742 1.00 36.83 N ATOM 1295 CA ALA 157 79.393 33.715 −13.559 1.00 36.83 C ATOM 1296 CB ALA 157 78.671 32.774 −12.585 1.00 36.83 C ATOM 1297 C ALA 157 79.626 33.015 −14.887 1.00 36.83 C ATOM 1298 O ALA 157 80.754 32.624 −15.209 1.00 36.83 O ATOM 1299 N ILE 158 78.553 32.858 −15.654 1.00 36.83 N ATOM 1300 CA ILE 158 78.619 32.204 −16.950 1.00 36.83 C ATOM 1301 CB ILE 158 77.200 32.054 −17.569 1.00 36.83 C ATOM 1302 CG2 ILE 158 76.636 33.416 −17.933 1.00 36.83 C ATOM 1303 CG1 ILE 158 77.258 31.191 −18.822 1.00 36.83 C ATOM 1304 CD1 ILE 158 77.554 29.717 −18.539 1.00 36.83 C ATOM 1305 C ILE 158 79.524 33.012 −17.880 1.00 36.83 C ATOM 1306 O ILE 158 80.157 32.455 −18.789 1.00 36.83 O ATOM 1307 N SER 159 79.588 34.324 −17.662 1.00 36.83 N ATOM 1308 CA SER 159 80.452 35.166 −18.480 1.00 36.83 C ATOM 1309 CB SER 159 80.175 36.650 −18.235 1.00 36.83 C ATOM 1310 OG SER 159 78.873 37.024 −18.635 1.00 36.83 O ATOM 1311 C SER 159 81.908 34.886 −18.111 1.00 36.83 C ATOM 1312 O SER 159 82.763 34.706 −18.977 1.00 36.83 O ATOM 1313 N ASP 160 82.167 34.848 −16.808 1.00 36.83 N ATOM 1314 CA ASP 160 83.503 34.617 −16.272 1.00 36.83 C ATOM 1315 CB ASP 160 83.452 34.672 −14.734 1.00 36.83 C ATOM 1316 CG ASP 160 84.828 34.671 −14.100 1.00 36.83 C ATOM 1317 OD1 ASP 160 85.327 33.566 −13.773 1.00 36.83 O ATOM 1318 OD2 ASP 160 85.415 35.776 −13.942 1.00 36.83 O ATOM 1319 C ASP 160 84.060 33.285 −16.758 1.00 36.83 C ATOM 1320 O ASP 160 85.228 33.196 −17.147 1.00 36.83 O ATOM 1321 N VAL 161 83.216 32.257 −16.753 1.00 36.83 N ATOM 1322 CA VAL 161 83.631 30.942 −17.209 1.00 36.83 C ATOM 1323 CB VAL 161 82.528 29.889 −16.998 1.00 36.83 C ATOM 1324 CG1 VAL 161 83.046 28.534 −17.386 1.00 36.83 C ATOM 1325 CG2 VAL 161 82.077 29.874 −15.553 1.00 36.83 C ATOM 1326 C VAL 161 83.992 30.980 −18.699 1.00 36.83 C ATOM 1327 O VAL 161 84.959 30.344 −19.129 1.00 36.83 O ATOM 1328 N ALA 162 83.221 31.718 −19.492 1.00 36.83 N ATOM 1329 CA ALA 162 83.527 31.793 −20.909 1.00 36.83 C ATOM 1330 CB ALA 162 82.396 32.461 −21.668 1.00 36.83 C ATOM 1331 C ALA 162 84.824 32.582 −21.094 1.00 36.83 C ATOM 1332 O ALA 162 85.556 32.381 −22.064 1.00 36.83 O ATOM 1333 N TYR 163 85.105 33.477 −20.151 1.00 36.83 N ATOM 1334 CA TYR 163 86.306 34.284 −20.241 1.00 36.83 C ATOM 1335 CB TYR 163 86.218 35.467 −19.282 1.00 36.83 C ATOM 1336 CG TYR 163 87.451 36.357 −19.280 1.00 36.83 C ATOM 1337 CD1 TYR 163 87.802 37.115 −20.402 1.00 36.83 C ATOM 1338 CE1 TYR 163 88.900 37.965 −20.374 1.00 36.83 C ATOM 1339 CD2 TYR 163 88.239 36.472 −18.140 1.00 36.83 C ATOM 1340 CE2 TYR 163 89.330 37.310 −18.103 1.00 36.83 C ATOM 1341 CZ TYR 163 89.654 38.058 −19.214 1.00 36.83 C ATOM 1342 OH TYR 163 90.704 38.941 −19.127 1.00 36.83 O ATOM 1343 C TYR 163 87.549 33.463 −19.934 1.00 36.83 C ATOM 1344 O TYR 163 88.537 33.530 −20.661 1.00 36.83 O ATOM 1345 N ARG 164 87.490 32.691 −18.857 1.00 36.83 N ATOM 1346 CA ARG 164 88.621 31.870 −18.446 1.00 36.83 C ATOM 1347 CB ARG 164 88.302 31.114 −17.143 1.00 36.83 C ATOM 1348 CG ARG 164 87.826 32.006 −16.013 1.00 36.83 C ATOM 1349 CD ARG 164 88.872 33.044 −15.632 1.00 36.83 C ATOM 1350 NE ARG 164 88.254 34.333 −15.326 1.00 36.83 N ATOM 1351 CZ ARG 164 88.869 35.330 −14.703 1.00 36.83 C ATOM 1352 NH1 ARG 164 90.128 35.186 −14.310 1.00 36.83 N ATOM 1353 NH2 ARG 164 88.233 36.469 −14.475 1.00 36.83 N ATOM 1354 C ARG 164 88.985 30.875 −19.535 1.00 36.83 C ATOM 1355 O ARG 164 90.156 30.718 −19.887 1.00 36.83 O ATOM 1356 N SER 165 87.966 30.214 −20.070 1.00 36.83 N ATOM 1357 CA SER 165 88.152 29.212 −21.112 1.00 36.83 C ATOM 1358 CB SER 165 86.803 28.646 −21.506 1.00 36.83 C ATOM 1359 OG SER 165 86.173 28.115 −20.361 1.00 36.83 O ATOM 1360 C SER 165 88.856 29.787 −22.329 1.00 36.83 C ATOM 1361 O SER 165 89.656 29.105 −22.974 1.00 36.83 O ATOM 1362 N MET 166 88.534 31.033 −22.658 1.00 36.83 N ATOM 1363 CA MET 166 89.182 31.696 −23.766 1.00 36.83 C ATOM 1364 CB MET 166 88.624 33.103 −23.966 1.00 36.83 C ATOM 1365 CG MET 166 89.276 33.826 −25.118 1.00 36.83 C ATOM 1366 SD MET 166 88.821 35.556 −25.224 1.00 36.83 S ATOM 1367 CE MET 166 89.782 36.201 −23.901 1.00 36.83 C ATOM 1368 C MET 166 90.664 31.800 −23.414 1.00 36.83 C ATOM 1369 O MET 166 91.535 31.516 −24.241 1.00 36.83 O ATOM 1370 N LEU 167 90.947 32.182 −22.170 1.00 36.83 N ATOM 1371 CA LEU 167 92.331 32.341 −21.724 1.00 36.83 C ATOM 1372 CB LEU 167 92.410 33.292 −20.519 1.00 36.83 C ATOM 1373 CG LEU 167 91.878 34.714 −20.688 1.00 36.83 C ATOM 1374 CD1 LEU 167 92.288 35.569 −19.504 1.00 36.83 C ATOM 1375 CD2 LEU 167 92.425 35.305 −21.963 1.00 36.83 C ATOM 1376 C LEU 167 93.038 31.049 −21.364 1.00 36.83 C ATOM 1377 O LEU 167 94.269 31.000 −21.371 1.00 36.83 O ATOM 1378 N ASP 168 92.284 30.000 −21.054 1.00 36.83 N ATOM 1379 CA ASP 168 92.902 28.732 −20.665 1.00 36.83 C ATOM 1380 CB ASP 168 92.141 28.126 −19.472 1.00 36.83 C ATOM 1381 CG ASP 168 92.255 28.984 −18.219 1.00 36.83 C ATOM 1382 OD1 ASP 168 93.135 29.874 −18.208 1.00 36.83 O ATOM 1383 OD2 ASP 168 91.487 28.783 −17.243 1.00 36.83 O ATOM 1384 C ASP 168 93.009 27.721 −21.806 1.00 36.83 C ATOM 1385 O ASP 168 93.858 26.820 −21.784 1.00 36.83 O ATOM 1386 N ASP 169 92.159 27.864 −22.811 1.00 36.83 N ATOM 1387 CA ASP 169 92.196 26.948 −23.934 1.00 36.83 C ATOM 1388 CB ASP 169 90.809 26.352 −24.184 1.00 36.83 C ATOM 1389 CG ASP 169 90.315 25.511 −23.016 1.00 36.83 C ATOM 1390 OD1 ASP 169 91.156 24.924 −22.313 1.00 36.83 O ATOM 1391 OD2 ASP 169 89.082 25.422 −22.814 1.00 36.83 O ATOM 1392 C ASP 169 92.684 27.648 −25.187 1.00 36.83 C ATOM 1393 O ASP 169 93.007 27.002 −26.180 1.00 36.83 O ATOM 1394 N ARG 170 92.743 28.974 −25.135 1.00 36.83 N ATOM 1395 CA ARG 170 93.173 29.761 −26.287 1.00 36.83 C ATOM 1396 CB ARG 170 94.535 29.269 −26.781 1.00 36.83 C ATOM 1397 CG ARG 170 95.664 29.357 −25.751 1.00 36.83 C ATOM 1398 CD ARG 170 96.117 30.797 −25.555 1.00 36.83 C ATOM 1399 NE ARG 170 97.452 30.879 −24.958 1.00 36.83 N ATOM 1400 CZ ARG 170 97.770 30.451 −23.732 1.00 36.83 C ATOM 1401 NH1 ARG 170 96.855 29.898 −22.935 1.00 36.83 N ATOM 1402 NH2 ARG 170 99.015 30.565 −23.302 1.00 36.83 N ATOM 1403 C ARG 170 92.145 29.647 −27.420 1.00 36.83 C ATOM 1404 O ARG 170 92.447 29.966 −28.570 1.00 36.83 O ATOM 1405 N GLN 171 90.931 29.206 −27.081 1.00 36.83 N ATOM 1406 CA GLN 171 89.850 29.021 −28.053 1.00 36.83 C ATOM 1407 CB GLN 171 89.250 27.616 −27.883 1.00 36.83 C ATOM 1408 CG GLN 171 88.210 27.243 −28.921 1.00 36.83 C ATOM 1409 CD GLN 171 87.917 25.743 −28.968 1.00 36.83 C ATOM 1410 OE1 GLN 171 88.831 24.919 −29.152 1.00 36.83 O ATOM 1411 NE2 GLN 171 86.635 25.379 −28.821 1.00 36.83 N ATOM 1412 C GLN 171 88.744 30.076 −27.923 1.00 36.83 C ATOM 1413 O GLN 171 88.335 30.428 −26.808 1.00 36.83 O ATOM 1414 N ASN 172 88.270 30.573 −29.067 1.00 36.83 N ATOM 1415 CA ASN 172 87.204 31.579 −29.112 1.00 36.83 C ATOM 1416 CB ASN 172 86.895 31.955 −30.569 1.00 36.83 C ATOM 1417 CG ASN 172 87.976 32.810 −31.199 1.00 36.83 C ATOM 1418 OD1 ASN 172 88.493 32.485 −32.274 1.00 36.83 O ATOM 1419 ND2 ASN 172 88.312 33.925 −30.546 1.00 36.83 N ATOM 1420 C ASN 172 85.925 31.043 −28.454 1.00 36.83 C ATOM 1421 O ASN 172 85.633 29.854 −28.514 1.00 36.83 O ATOM 1422 N GLN 173 85.150 31.926 −27.844 1.00 36.83 N ATOM 1423 CA GLN 173 83.927 31.496 −27.166 1.00 36.83 C ATOM 1424 CB GLN 173 84.082 31.687 −25.648 1.00 36.83 C ATOM 1425 CG GLN 173 85.373 31.152 −25.039 1.00 36.83 C ATOM 1426 CD GLN 173 85.373 29.649 −24.861 1.00 36.83 C ATOM 1427 OE1 GLN 173 84.398 29.068 −24.395 1.00 36.83 O ATOM 1428 NE2 GLN 173 86.490 29.008 −25.217 1.00 36.83 N ATOM 1429 C GLN 173 82.695 32.269 −27.640 1.00 36.83 C ATOM 1430 O GLN 173 82.807 33.290 −28.332 1.00 36.83 O ATOM 1431 N SER 174 81.518 31.780 −27.257 1.00 36.83 N ATOM 1432 CA SER 174 80.265 32.448 −27.626 1.00 36.83 C ATOM 1433 CB SER 174 79.763 31.961 −28.988 1.00 36.83 C ATOM 1434 OG SER 174 79.309 30.621 −28.909 1.00 36.83 O ATOM 1435 C SER 174 79.150 32.244 −26.608 1.00 36.83 C ATOM 1436 O SER 174 78.958 31.142 −26.074 1.00 36.83 O ATOM 1437 N LEU 175 78.426 33.320 −26.332 1.00 36.83 N ATOM 1438 CA LEU 175 77.297 33.256 −25.421 1.00 36.83 C ATOM 1439 CB LEU 175 77.360 34.381 −24.387 1.00 36.83 C ATOM 1440 CG LEU 175 78.220 34.033 −23.172 1.00 36.83 C ATOM 1441 CD1 LEU 175 79.641 33.760 −23.606 1.00 36.83 C ATOM 1442 CD2 LEU 175 78.182 35.157 −22.178 1.00 36.83 C ATOM 1443 C LEU 175 76.013 33.347 −26.235 1.00 36.83 C ATOM 1444 O LEU 175 75.655 34.395 −26.756 1.00 36.83 O ATOM 1445 N LEU 176 75.341 32.217 −26.357 1.00 36.83 N ATOM 1446 CA LEU 176 74.097 32.144 −27.093 1.00 36.83 C ATOM 1447 CB LEU 176 74.043 30.814 −27.844 1.00 36.83 C ATOM 1448 CG LEU 176 75.332 30.575 −28.639 1.00 36.83 C ATOM 1449 CD1 LEU 176 75.256 29.264 −29.348 1.00 36.83 C ATOM 1450 CD2 LEU 176 75.558 31.690 −29.637 1.00 36.83 C ATOM 1451 C LEU 176 72.929 32.271 −26.114 1.00 36.83 C ATOM 1452 O LEU 176 72.702 31.398 −25.281 1.00 36.83 O ATOM 1453 N ILE 177 72.188 33.365 −26.217 1.00 36.83 N ATOM 1454 CA ILE 177 71.060 33.578 −25.321 1.00 36.83 C ATOM 1455 CB ILE 177 71.144 34.970 −24.644 1.00 36.83 C ATOM 1456 CG2 ILE 177 70.106 35.063 −23.517 1.00 36.83 C ATOM 1457 CG1 ILE 177 72.566 35.180 −24.102 1.00 36.83 C ATOM 1458 CD1 ILE 177 72.797 36.512 −23.477 1.00 36.83 C ATOM 1459 C ILE 177 69.737 33.437 −26.065 1.00 36.83 C ATOM 1460 O ILE 177 69.342 34.308 −26.832 1.00 36.83 O ATOM 1461 N THR 178 69.063 32.322 −25.824 1.00 36.83 N ATOM 1462 CA THR 178 67.795 32.039 −26.473 1.00 36.83 C ATOM 1463 CB THR 178 67.622 30.511 −26.693 1.00 36.83 C ATOM 1464 OG1 THR 178 67.320 29.876 −25.449 1.00 36.83 O ATOM 1465 CG2 THR 178 68.899 29.912 −27.245 1.00 36.83 C ATOM 1466 C THR 178 66.577 32.558 −25.699 1.00 36.83 C ATOM 1467 O THR 178 66.674 32.950 −24.539 1.00 36.83 O ATOM 1468 N GLY 179 65.428 32.554 −26.362 1.00 36.83 N ATOM 1469 CA GLY 179 64.203 32.990 −25.720 1.00 36.83 C ATOM 1470 C GLY 179 63.164 33.561 −26.663 1.00 36.83 C ATOM 1471 O GLY 179 63.504 34.175 −27.666 1.00 36.83 O ATOM 1472 N GLU 180 61.890 33.338 −26.354 1.00 36.83 N ATOM 1473 CA GLU 180 60.826 33.883 −27.171 1.00 36.83 C ATOM 1474 CB GLU 180 59.471 33.258 −26.804 1.00 36.83 C ATOM 1475 CG GLU 180 58.841 33.659 −25.464 1.00 36.83 C ATOM 1476 CD GLU 180 57.466 32.999 −25.257 1.00 36.83 C ATOM 1477 OE1 GLU 180 57.423 31.810 −24.901 1.00 36.83 O ATOM 1478 OE2 GLU 180 56.426 33.662 −25.467 1.00 36.83 O ATOM 1479 C GLU 180 60.843 35.384 −26.901 1.00 36.83 C ATOM 1480 O GLU 180 61.547 35.844 −25.998 1.00 36.83 O ATOM 1481 N SER 181 60.087 36.153 −27.676 1.00 36.83 N ATOM 1482 CA SER 181 60.079 37.601 −27.495 1.00 36.83 C ATOM 1483 CB SER 181 59.089 38.261 −28.459 1.00 36.83 C ATOM 1484 OG SER 181 59.048 39.658 −28.239 1.00 36.83 O ATOM 1485 C SER 181 59.767 38.026 −26.069 1.00 36.83 C ATOM 1486 O SER 181 58.839 37.522 −25.455 1.00 36.83 O ATOM 1487 N GLY 182 60.569 38.946 −25.545 1.00 36.83 N ATOM 1488 CA GLY 182 60.361 39.442 −24.192 1.00 36.83 C ATOM 1489 C GLY 182 60.878 38.588 −23.041 1.00 36.83 C ATOM 1490 O GLY 182 60.670 38.926 −21.873 1.00 36.83 O ATOM 1491 N ALA 183 61.553 37.486 −23.357 1.00 36.83 N ATOM 1492 CA ALA 183 62.080 36.599 −22.325 1.00 36.83 C ATOM 1493 CB ALA 183 62.459 35.246 −22.944 1.00 36.83 C ATOM 1494 C ALA 183 63.267 37.177 −21.517 1.00 36.83 C ATOM 1495 O ALA 183 63.530 36.733 −20.405 1.00 36.83 O ATOM 1496 N GLY 184 63.974 38.161 −22.065 1.00 36.83 N ATOM 1497 CA GLY 184 65.084 38.761 −21.338 1.00 36.83 C ATOM 1498 C GLY 184 66.447 38.686 −22.000 1.00 36.83 C ATOM 1499 O GLY 184 67.454 39.019 −21.381 1.00 36.83 O ATOM 1500 N LYS 185 66.476 38.265 −23.258 1.00 36.83 N ATOM 1501 CA LYS 185 67.712 38.132 −24.022 1.00 36.83 C ATOM 1502 CB LYS 185 67.406 37.678 −25.451 1.00 36.83 C ATOM 1503 CG LYS 185 66.817 36.291 −25.579 1.00 36.83 C ATOM 1504 CD LYS 185 66.463 36.034 −27.020 1.00 36.83 C ATOM 1505 CE LYS 185 65.455 37.053 −27.545 1.00 36.83 C ATOM 1506 NZ LYS 185 64.057 36.832 −27.060 1.00 36.83 N ATOM 1507 C LYS 185 68.553 39.399 −24.099 1.00 36.83 C ATOM 1508 O LYS 185 69.756 39.375 −23.835 1.00 36.83 O ATOM 1509 N THR 186 67.927 40.501 −24.485 1.00 36.83 N ATOM 1510 CA THR 186 68.655 41.746 −24.605 1.00 36.83 C ATOM 1511 CB THR 186 67.778 42.834 −25.290 1.00 36.83 C ATOM 1512 OG1 THR 186 67.524 42.449 −26.645 1.00 36.83 O ATOM 1513 CG2 THR 186 68.481 44.179 −25.302 1.00 36.83 C ATOM 1514 C THR 186 69.202 42.244 −23.260 1.00 36.83 C ATOM 1515 O THR 186 70.359 42.652 −23.193 1.00 36.83 O ATOM 1516 N GLU 187 68.399 42.196 −22.195 1.00 36.83 N ATOM 1517 CA GLU 187 68.854 42.657 −20.880 1.00 36.83 C ATOM 1518 CB GLU 187 67.726 42.588 −19.844 1.00 36.83 C ATOM 1519 CG GLU 187 66.566 43.513 −20.135 1.00 36.83 C ATOM 1520 CD GLU 187 67.021 44.940 −20.332 1.00 36.83 C ATOM 1521 OE1 GLU 187 66.522 45.605 −21.263 1.00 36.83 O ATOM 1522 OE2 GLU 187 67.882 45.398 −19.554 1.00 36.83 O ATOM 1523 C GLU 187 70.042 41.845 −20.386 1.00 36.83 C ATOM 1524 O GLU 187 70.953 42.386 −19.739 1.00 36.83 O ATOM 1525 N ASN 188 70.026 40.548 −20.680 1.00 36.83 N ATOM 1526 CA ASN 188 71.113 39.677 −20.283 1.00 36.83 C ATOM 1527 CB ASN 188 70.664 38.219 −20.314 1.00 36.83 C ATOM 1528 CG ASN 188 69.978 37.801 −19.024 1.00 36.83 C ATOM 1529 OD1 ASN 188 70.631 37.586 −18.003 1.00 36.83 O ATOM 1530 ND2 ASN 188 68.655 37.705 −19.058 1.00 36.83 N ATOM 1531 C ASN 188 72.354 39.894 −21.145 1.00 36.83 C ATOM 1532 O ASN 188 73.461 39.716 −20.670 1.00 36.83 O ATOM 1533 N THR 189 72.166 40.289 −22.404 1.00 36.83 N ATOM 1534 CA THR 189 73.288 40.564 −23.290 1.00 36.83 C ATOM 1535 CB THR 189 72.837 40.846 −24.763 1.00 36.83 C ATOM 1536 OG1 THR 189 72.205 39.684 −25.324 1.00 36.83 O ATOM 1537 CG2 THR 189 74.039 41.194 −25.626 1.00 36.83 C ATOM 1538 C THR 189 73.999 41.804 −22.738 1.00 36.83 C ATOM 1539 O THR 189 75.226 41.827 −22.654 1.00 36.83 O ATOM 1540 N LYS 190 73.229 42.822 −22.345 1.00 36.83 N ATOM 1541 CA LYS 190 73.810 44.051 −21.790 1.00 36.83 C ATOM 1542 CB LYS 190 72.739 45.071 −21.393 1.00 36.83 C ATOM 1543 CG LYS 190 71.964 45.699 −22.520 1.00 36.83 C ATOM 1544 CD LYS 190 70.835 46.576 −21.949 1.00 36.83 C ATOM 1545 CE LYS 190 69.921 47.128 −23.038 1.00 36.83 C ATOM 1546 NZ LYS 190 68.785 47.886 −22.446 1.00 36.83 N ATOM 1547 C LYS 190 74.657 43.772 −20.548 1.00 36.83 C ATOM 1548 O LYS 190 75.640 44.479 −20.300 1.00 36.83 O ATOM 1549 N LYS 191 74.272 42.770 −19.760 1.00 36.83 N ATOM 1550 CA LYS 191 75.025 42.444 −18.567 1.00 36.83 C ATOM 1551 CB LYS 191 74.189 41.599 −17.600 1.00 36.83 C ATOM 1552 CG LYS 191 72.868 42.247 −17.185 1.00 36.83 C ATOM 1553 CD LYS 191 73.042 43.714 −16.793 1.00 36.83 C ATOM 1554 CE LYS 191 71.704 44.445 −16.770 1.00 36.83 C ATOM 1555 NZ LYS 191 71.059 44.473 −18.128 1.00 36.83 N ATOM 1556 C LYS 191 76.314 41.714 −18.925 1.00 36.83 C ATOM 1557 O LYS 191 77.346 41.923 −18.280 1.00 36.83 O ATOM 1558 N VAL 192 76.262 40.849 −19.937 1.00 36.83 N ATOM 1559 CA VAL 192 77.469 40.142 −20.345 1.00 36.83 C ATOM 1560 CB VAL 192 77.223 39.142 −21.500 1.00 36.83 C ATOM 1561 CG1 VAL 192 78.565 38.645 −22.037 1.00 36.83 C ATOM 1562 CG2 VAL 192 76.404 37.960 −21.007 1.00 36.83 C ATOM 1563 C VAL 192 78.484 41.184 −20.809 1.00 36.83 C ATOM 1564 O VAL 192 79.611 41.185 −20.342 1.00 36.83 O ATOM 1565 N ILE 193 78.083 42.072 −21.718 1.00 36.83 N ATOM 1566 CA ILE 193 78.997 43.108 −22.188 1.00 36.83 C ATOM 1567 CB ILE 193 78.304 44.122 −23.137 1.00 36.83 C ATOM 1568 CG2 ILE 193 79.335 45.101 −23.684 1.00 36.83 C ATOM 1569 CG1 ILE 193 77.619 43.398 −24.308 1.00 36.83 C ATOM 1570 CD1 ILE 193 78.519 42.432 −25.047 1.00 36.83 C ATOM 1571 C ILE 193 79.534 43.858 −20.954 1.00 36.83 C ATOM 1572 O ILE 193 80.737 43.957 −20.768 1.00 36.83 O ATOM 1573 N GLN 194 78.637 44.356 −20.107 1.00 36.83 N ATOM 1574 CA GLN 194 79.019 45.079 −18.887 1.00 36.83 C ATOM 1575 CB GLN 194 77.817 45.274 −17.960 1.00 36.83 C ATOM 1576 CG GLN 194 78.156 45.983 −16.651 1.00 36.83 C ATOM 1577 CD GLN 194 77.055 45.857 −15.622 1.00 36.83 C ATOM 1578 OE1 GLN 194 75.871 45.967 −15.951 1.00 36.83 O ATOM 1579 NE2 GLN 194 77.429 45.635 −14.375 1.00 36.83 N ATOM 1580 C GLN 194 80.098 44.365 −18.096 1.00 36.83 C ATOM 1581 O GLN 194 81.109 44.966 −17.731 1.00 36.83 O ATOM 1582 N TYR 195 79.880 43.086 −17.817 1.00 36.83 N ATOM 1583 CA TYR 195 80.852 42.301 −17.057 1.00 36.83 C ATOM 1584 CB TYR 195 80.328 40.900 −16.780 1.00 36.83 C ATOM 1585 CG TYR 195 81.212 40.089 −15.864 1.00 36.83 C ATOM 1586 CD1 TYR 195 81.161 40.273 −14.483 1.00 36.83 C ATOM 1587 CE1 TYR 195 81.919 39.489 −13.614 1.00 36.83 C ATOM 1588 CD2 TYR 195 82.058 39.102 −16.367 1.00 36.83 C ATOM 1589 CE2 TYR 195 82.832 38.306 −15.505 1.00 36.83 C ATOM 1590 CZ TYR 195 82.748 38.509 −14.126 1.00 36.83 C ATOM 1591 OH TYR 195 83.469 37.727 −13.252 1.00 36.83 O ATOM 1592 C TYR 195 82.176 42.174 −17.784 1.00 36.83 C ATOM 1593 O TYR 195 83.224 42.376 −17.182 1.00 36.83 O ATOM 1594 N LEU 196 82.132 41.820 −19.066 1.00 36.83 N ATOM 1595 CA LEU 196 83.348 41.667 −19.860 1.00 36.83 C ATOM 1596 CB LEU 196 83.012 41.254 −21.291 1.00 36.83 C ATOM 1597 CG LEU 196 82.812 39.760 −21.523 1.00 36.83 C ATOM 1598 CD1 LEU 196 81.811 39.225 −20.521 1.00 36.83 C ATOM 1599 CD2 LEU 196 82.344 39.522 −22.957 1.00 36.83 C ATOM 1600 C LEU 196 84.169 42.944 −19.901 1.00 36.83 C ATOM 1601 O LEU 196 85.389 42.902 −19.824 1.00 36.83 O ATOM 1602 N ALA 197 83.490 44.076 −20.025 1.00 36.83 N ATOM 1603 CA ALA 197 84.153 45.364 −20.087 1.00 36.83 C ATOM 1604 CB ALA 197 83.132 46.444 −20.362 1.00 36.83 C ATOM 1605 C ALA 197 84.898 45.684 −18.793 1.00 36.83 C ATOM 1606 O ALA 197 85.914 46.394 −18.793 1.00 36.83 O ATOM 1607 N SER 198 84.389 45.168 −17.683 1.00 36.83 N ATOM 1608 CA SER 198 84.995 45.443 −16.401 1.00 36.83 C ATOM 1609 CB SER 198 83.911 45.470 −15.327 1.00 36.83 C ATOM 1610 OG SER 198 84.455 45.718 −14.048 1.00 36.83 O ATOM 1611 C SER 198 86.084 44.442 −16.042 1.00 36.83 C ATOM 1612 O SER 198 87.223 44.823 −15.780 1.00 36.83 O ATOM 1613 N VAL 199 85.746 43.161 −16.053 1.00 36.83 N ATOM 1614 CA VAL 199 86.707 42.131 −15.709 1.00 36.83 C ATOM 1615 CB VAL 199 86.034 40.748 −15.776 1.00 36.83 C ATOM 1616 CG1 VAL 199 86.117 40.184 −17.186 1.00 36.83 C ATOM 1617 CG2 VAL 199 86.653 39.813 −14.758 1.00 36.83 C ATOM 1618 C VAL 199 87.950 42.168 −16.610 1.00 36.83 C ATOM 1619 O VAL 199 88.983 41.581 −16.270 1.00 36.83 O ATOM 1620 N ALA 200 87.859 42.875 −17.743 1.00 36.83 N ATOM 1621 CA ALA 200 88.980 42.975 −18.689 1.00 36.83 C ATOM 1622 CB ALA 200 88.732 42.047 −19.881 1.00 36.83 C ATOM 1623 C ALA 200 89.313 44.398 −19.196 1.00 36.83 C ATOM 1624 O ALA 200 89.948 44.552 −20.244 1.00 36.83 O ATOM 1625 N GLY 201 88.882 45.426 −18.470 1.00 36.83 N ATOM 1626 CA GLY 201 89.179 46.800 −18.863 1.00 36.83 C ATOM 1627 C GLY 201 90.656 47.148 −18.681 1.00 36.83 C ATOM 1628 O GLY 201 91.457 46.263 −18.355 1.00 36.83 O ATOM 1629 N ARG 202 91.042 48.417 −18.864 1.00 36.83 N ATOM 1630 CA ARG 202 92.465 48.779 −18.726 1.00 36.83 C ATOM 1631 CB ARG 202 92.832 49.875 −19.742 1.00 36.83 C ATOM 1632 CG ARG 202 93.030 49.368 −21.189 1.00 36.83 C ATOM 1633 CD ARG 202 94.121 48.273 −21.313 1.00 36.83 C ATOM 1634 NE ARG 202 94.345 47.871 −22.708 1.00 36.83 N ATOM 1635 CZ ARG 202 95.294 47.025 −23.122 1.00 36.83 C ATOM 1636 NH1 ARG 202 96.136 46.470 −22.256 1.00 36.83 N ATOM 1637 NH2 ARG 202 95.395 46.729 −24.415 1.00 36.83 N ATOM 1638 C ARG 202 93.014 49.167 −17.327 1.00 36.83 C ATOM 1639 O ARG 202 92.352 49.005 −16.292 1.00 36.83 O ATOM 1640 N ASN 203 94.249 49.666 −17.317 0.00 36.83 N ATOM 1641 CA ASN 203 94.932 50.058 −16.081 0.00 36.83 C ATOM 1642 CB ASN 203 96.431 49.768 −16.202 0.00 36.83 C ATOM 1643 CG ASN 203 96.721 48.321 −16.544 0.00 36.83 C ATOM 1644 OD1 ASN 203 96.363 47.410 −15.798 0.00 36.83 O ATOM 1645 ND2 ASN 203 97.374 48.102 −17.680 0.00 36.83 N ATOM 1646 C ASN 203 94.733 51.527 −15.711 0.00 36.83 C ATOM 1647 O ASN 203 93.603 51.987 −15.562 0.00 36.83 O ATOM 1648 N GLN 204 95.840 52.253 −15.551 1.00 36.83 N ATOM 1649 CA GLN 204 95.792 53.676 −15.199 1.00 36.83 C ATOM 1650 CB GLN 204 96.525 53.918 −13.870 1.00 36.83 C ATOM 1651 CG GLN 204 98.038 53.721 −13.943 1.00 36.83 C ATOM 1652 CD GLN 204 98.427 52.499 −14.771 1.00 36.83 C ATOM 1653 OE1 GLN 204 98.282 52.493 −16.003 1.00 36.83 O ATOM 1654 NE2 GLN 204 98.921 51.452 −14.095 1.00 36.83 N ATOM 1655 C GLN 204 96.404 54.572 −16.286 1.00 36.83 C ATOM 1656 O GLN 204 96.765 54.102 −17.382 1.00 36.83 O ATOM 1657 N ALA 205 96.521 55.860 −15.962 1.00 36.83 N ATOM 1658 CA ALA 205 97.084 56.878 −16.863 1.00 36.83 C ATOM 1659 CB ALA 205 98.409 56.392 −17.444 1.00 36.83 C ATOM 1660 C ALA 205 96.134 57.248 −18.000 1.00 36.83 C ATOM 1661 O ALA 205 95.241 58.094 −17.847 1.00 36.83 O ATOM 1662 N ASN 206 96.339 56.589 −19.134 0.00 36.83 N ATOM 1663 CA ASN 206 95.558 56.798 −20.346 0.00 36.83 C ATOM 1664 CB ASN 206 96.507 56.828 −21.533 0.00 36.83 C ATOM 1665 CG ASN 206 97.468 55.659 −21.517 0.00 36.83 C ATOM 1666 OD1 ASN 206 97.057 54.503 −21.629 0.00 36.83 O ATOM 1667 ND2 ASN 206 98.753 55.948 −21.359 0.00 36.83 N ATOM 1668 C ASN 206 94.555 55.665 −20.529 0.00 36.83 C ATOM 1669 O ASN 206 94.654 54.633 −19.867 0.00 36.83 O ATOM 1670 N GLY 207 93.605 55.858 −21.442 1.00 36.83 N ATOM 1671 CA GLY 207 92.594 54.840 −21.700 1.00 36.83 C ATOM 1672 C GLY 207 91.916 54.404 −20.419 1.00 36.83 C ATOM 1673 O GLY 207 90.827 54.886 −20.077 1.00 36.83 O ATOM 1674 N SER 208 92.566 53.488 −19.704 1.00 36.83 N ATOM 1675 CA SER 208 92.061 52.980 −18.421 1.00 36.83 C ATOM 1676 CB SER 208 92.187 54.063 −17.341 1.00 36.83 C ATOM 1677 OG SER 208 91.889 53.545 −16.048 1.00 36.83 O ATOM 1678 C SER 208 90.612 52.510 −18.496 1.00 36.83 C ATOM 1679 O SER 208 90.074 51.976 −17.517 1.00 36.83 O ATOM 1680 N GLY 209 90.001 52.711 −19.664 1.00 36.83 N ATOM 1681 CA GLY 209 88.619 52.330 −19.894 1.00 36.83 C ATOM 1682 C GLY 209 87.936 53.223 −20.922 1.00 36.83 C ATOM 1683 O GLY 209 86.763 53.564 −20.770 1.00 36.83 O ATOM 1684 N VAL 210 88.641 53.613 −21.974 1.00 36.83 N ATOM 1685 CA VAL 210 88.017 54.473 −22.979 1.00 36.83 C ATOM 1686 CB VAL 210 89.064 55.318 −23.741 1.00 36.83 C ATOM 1687 CG1 VAL 210 88.352 56.158 −24.822 1.00 36.83 C ATOM 1688 CG2 VAL 210 89.813 56.226 −22.766 1.00 36.83 C ATOM 1689 C VAL 210 87.200 53.668 −23.999 1.00 36.83 C ATOM 1690 O VAL 210 86.012 53.908 −24.189 1.00 36.83 O ATOM 1691 N LEU 211 87.859 52.734 −24.673 1.00 36.83 N ATOM 1692 CA LEU 211 87.190 51.873 −25.642 1.00 36.83 C ATOM 1693 CB LEU 211 88.154 50.771 −26.102 1.00 36.83 C ATOM 1694 CG LEU 211 88.018 50.159 −27.497 1.00 36.83 C ATOM 1695 CD1 LEU 211 88.980 48.985 −27.617 1.00 36.83 C ATOM 1696 CD2 LEU 211 86.598 49.687 −27.736 1.00 36.83 C ATOM 1697 C LEU 211 86.026 51.257 −24.851 1.00 36.83 C ATOM 1698 O LEU 211 84.895 51.145 −25.336 1.00 36.83 O ATOM 1699 N GLU 212 86.325 50.895 −23.609 1.00 36.83 N ATOM 1700 CA GLU 212 85.354 50.287 −22.712 1.00 36.83 C ATOM 1701 CB GLU 212 85.935 50.201 −21.299 1.00 36.83 C ATOM 1702 CG GLU 212 86.906 49.048 −21.051 1.00 36.83 C ATOM 1703 CD GLU 212 88.251 49.190 −21.765 1.00 36.83 C ATOM 1704 OE1 GLU 212 88.830 50.303 −21.754 1.00 36.83 O ATOM 1705 OE2 GLU 212 88.738 48.173 −22.317 1.00 36.83 O ATOM 1706 C GLU 212 83.996 50.995 −22.663 1.00 36.83 C ATOM 1707 O GLU 212 82.963 50.344 −22.814 1.00 36.83 O ATOM 1708 N GLN 213 83.986 52.311 −22.454 1.00 36.83 N ATOM 1709 CA GLN 213 82.723 53.050 −22.381 1.00 36.83 C ATOM 1710 CB GLN 213 82.937 54.445 −21.774 1.00 36.83 C ATOM 1711 CG GLN 213 82.972 54.492 −20.231 1.00 36.83 C ATOM 1712 CD GLN 213 81.597 54.351 −19.578 1.00 36.83 C ATOM 1713 OE1 GLN 213 80.693 55.179 −19.802 1.00 36.83 O ATOM 1714 NE2 GLN 213 81.430 53.304 −18.758 1.00 36.83 N ATOM 1715 C GLN 213 82.014 53.200 −23.721 1.00 36.83 C ATOM 1716 O GLN 213 80.785 53.326 −23.778 1.00 36.83 O ATOM 1717 N GLN 214 82.784 53.202 −24.800 1.00 36.83 N ATOM 1718 CA GLN 214 82.205 53.335 −26.122 1.00 36.83 C ATOM 1719 CB GLN 214 83.301 53.675 −27.123 1.00 36.83 C ATOM 1720 CG GLN 214 84.051 54.921 −26.705 1.00 36.83 C ATOM 1721 CD GLN 214 85.036 55.398 −27.742 1.00 36.83 C ATOM 1722 OE1 GLN 214 85.964 54.681 −28.109 1.00 36.83 O ATOM 1723 NE2 GLN 214 84.841 56.620 −28.219 1.00 36.83 N ATOM 1724 C GLN 214 81.508 52.033 −26.486 1.00 36.83 C ATOM 1725 O GLN 214 80.455 52.033 −27.127 1.00 36.83 O ATOM 1726 N ILE 215 82.097 50.918 −26.068 1.00 36.83 N ATOM 1727 CA ILE 215 81.503 49.625 −26.339 1.00 36.83 C ATOM 1728 CB ILE 215 82.347 48.490 −25.746 1.00 36.83 C ATOM 1729 CG2 ILE 215 81.608 47.153 −25.902 1.00 36.83 C ATOM 1730 CG1 ILE 215 83.704 48.451 −26.445 1.00 36.83 C ATOM 1731 CD1 ILE 215 84.510 47.204 −26.190 1.00 36.83 C ATOM 1732 C ILE 215 80.126 49.614 −25.699 1.00 36.83 C ATOM 1733 O ILE 215 79.144 49.208 −26.318 1.00 36.83 O ATOM 1734 N LEU 216 80.059 50.083 −24.457 1.00 36.83 N ATOM 1735 CA LEU 216 78.809 50.137 −23.719 1.00 36.83 C ATOM 1736 CB LEU 216 79.065 50.602 −22.288 1.00 36.83 C ATOM 1737 CG LEU 216 79.945 49.733 −21.384 1.00 36.83 C ATOM 1738 CD1 LEU 216 80.145 50.456 −20.061 1.00 36.83 C ATOM 1739 CD2 LEU 216 79.297 48.378 −21.152 1.00 36.83 C ATOM 1740 C LEU 216 77.816 51.078 −24.363 1.00 36.83 C ATOM 1741 O LEU 216 76.635 50.759 −24.526 1.00 36.83 O ATOM 1742 N GLN 217 78.301 52.248 −24.740 1.00 36.83 N ATOM 1743 CA GLN 217 77.438 53.263 −25.329 1.00 36.83 C ATOM 1744 CB GLN 217 78.195 54.592 −25.413 1.00 36.83 C ATOM 1745 CG GLN 217 77.290 55.795 −25.154 1.00 36.83 C ATOM 1746 CD GLN 217 76.847 55.909 −23.703 1.00 36.83 C ATOM 1747 OE1 GLN 217 75.916 56.651 −23.388 1.00 36.83 O ATOM 1748 NE2 GLN 217 77.521 55.182 −22.809 1.00 36.83 N ATOM 1749 C GLN 217 76.849 52.898 −26.689 1.00 36.83 C ATOM 1750 O GLN 217 75.867 53.495 −27.123 1.00 36.83 O ATOM 1751 N ALA 218 77.442 51.919 −27.360 1.00 36.83 N ATOM 1752 CA ALA 218 76.951 51.475 −28.655 1.00 36.83 C ATOM 1753 CB ALA 218 77.756 50.270 −29.117 1.00 36.83 C ATOM 1754 C ALA 218 75.465 51.104 −28.563 1.00 36.83 C ATOM 1755 O ALA 218 74.649 51.517 −29.393 1.00 36.83 O ATOM 1756 N ASN 219 75.123 50.336 −27.532 1.00 36.83 N ATOM 1757 CA ASN 219 73.761 49.869 −27.309 1.00 36.83 C ATOM 1758 CB ASN 219 73.678 49.134 −25.967 1.00 36.83 C ATOM 1759 CG ASN 219 72.432 48.297 −25.859 1.00 36.83 C ATOM 1760 OD1 ASN 219 72.464 47.074 −26.046 1.00 36.83 O ATOM 1761 ND2 ASN 219 71.311 48.951 −25.592 1.00 36.83 N ATOM 1762 C ASN 219 72.645 50.927 −27.373 1.00 36.83 C ATOM 1763 O ASN 219 71.733 50.818 −28.191 1.00 36.83 O ATOM 1764 N PRO 220 72.687 51.950 −26.506 1.00 36.83 N ATOM 1765 CD PRO 220 73.645 52.260 −25.429 1.00 36.83 C ATOM 1766 CA PRO 220 71.631 52.963 −26.554 1.00 36.83 C ATOM 1767 CB PRO 220 72.119 54.017 −25.558 1.00 36.83 C ATOM 1768 CG PRO 220 72.836 53.203 −24.547 1.00 36.83 C ATOM 1769 C PRO 220 71.413 53.539 −27.950 1.00 36.83 C ATOM 1770 O PRO 220 70.294 53.914 −28.311 1.00 36.83 O ATOM 1771 N ILE 221 72.470 53.627 −28.742 1.00 36.83 N ATOM 1772 CA ILE 221 72.286 54.162 −30.077 1.00 36.83 C ATOM 1773 CB ILE 221 73.618 54.340 −30.814 1.00 36.83 C ATOM 1774 CG2 ILE 221 73.361 54.727 −32.255 1.00 36.83 C ATOM 1775 CG1 ILE 221 74.453 55.418 −30.119 1.00 36.83 C ATOM 1776 CD1 ILE 221 75.833 55.616 −30.733 1.00 36.83 C ATOM 1777 C ILE 221 71.416 53.183 −30.848 1.00 36.83 C ATOM 1778 O ILE 221 70.311 53.521 −31.270 1.00 36.83 O ATOM 1779 N LEU 222 71.903 51.958 −30.997 1.00 36.83 N ATOM 1780 CA LEU 222 71.164 50.937 −31.727 1.00 36.83 C ATOM 1781 CB LEU 222 71.940 49.620 −31.721 1.00 36.83 C ATOM 1782 CG LEU 222 73.267 49.620 −32.482 1.00 36.83 C ATOM 1783 CD1 LEU 222 73.762 48.197 −32.596 1.00 36.83 C ATOM 1784 CD2 LEU 222 73.086 50.178 −33.877 1.00 36.83 C ATOM 1785 C LEU 222 69.749 50.716 −31.203 1.00 36.83 C ATOM 1786 O LEU 222 68.795 50.634 −31.977 1.00 36.83 O ATOM 1787 N GLU 223 69.604 50.651 −29.887 1.00 36.83 N ATOM 1788 CA GLU 223 68.296 50.429 −29.290 1.00 36.83 C ATOM 1789 CB GLU 223 68.430 50.411 −27.768 1.00 36.83 C ATOM 1790 CG GLU 223 67.293 49.716 −27.043 1.00 36.83 C ATOM 1791 CD GLU 223 67.801 48.874 −25.874 1.00 36.83 C ATOM 1792 OE1 GLU 223 67.386 49.135 −24.731 1.00 36.83 O ATOM 1793 OE2 GLU 223 68.619 47.950 −26.105 1.00 36.83 O ATOM 1794 C GLU 223 67.265 51.478 −29.706 1.00 36.83 C ATOM 1795 O GLU 223 66.104 51.151 −29.962 1.00 36.83 O ATOM 1796 N ALA 224 67.682 52.740 −29.772 1.00 36.83 N ATOM 1797 CA ALA 224 66.766 53.808 −30.144 1.00 36.83 C ATOM 1798 CB ALA 224 67.451 55.179 −29.999 1.00 36.83 C ATOM 1799 C ALA 224 66.223 53.637 −31.559 1.00 36.83 C ATOM 1800 O ALA 224 65.037 53.895 −31.801 1.00 36.83 O ATOM 1801 N PHE 225 67.073 53.188 −32.483 1.00 36.83 N ATOM 1802 CA PHE 225 66.662 53.002 −33.874 1.00 36.83 C ATOM 1803 CB PHE 225 67.797 53.395 −34.834 1.00 36.83 C ATOM 1804 CG PHE 225 68.254 54.828 −34.702 1.00 36.83 C ATOM 1805 CD1 PHE 225 69.057 55.224 −33.633 1.00 36.83 C ATOM 1806 CD2 PHE 225 67.893 55.779 −35.660 1.00 36.83 C ATOM 1807 CE1 PHE 225 69.494 56.546 −33.524 1.00 36.83 C ATOM 1808 CE2 PHE 225 68.324 57.102 −35.560 1.00 36.83 C ATOM 1809 CZ PHE 225 69.125 57.486 −34.493 1.00 36.83 C ATOM 1810 C PHE 225 66.215 51.580 −34.227 1.00 36.83 C ATOM 1811 O PHE 225 65.475 51.379 −35.192 1.00 36.83 O ATOM 1812 N GLY 226 66.670 50.596 −33.453 1.00 36.83 N ATOM 1813 CA GLY 226 66.310 49.217 −33.732 1.00 36.83 C ATOM 1814 C GLY 226 65.250 48.578 −32.851 1.00 36.83 C ATOM 1815 O GLY 226 64.865 47.432 −33.098 1.00 36.83 O ATOM 1816 N ASN 227 64.778 49.293 −31.832 1.00 36.83 N ATOM 1817 CA ASN 227 63.759 48.755 −30.932 1.00 36.83 C ATOM 1818 CB ASN 227 64.263 48.749 −29.480 1.00 36.83 C ATOM 1819 CG ASN 227 65.354 47.698 −29.234 1.00 36.83 C ATOM 1820 OD1 ASN 227 66.299 47.578 −30.006 1.00 36.83 O ATOM 1821 ND2 ASN 227 65.221 46.945 −28.146 1.00 36.83 N ATOM 1822 C ASN 227 62.431 49.504 −31.014 1.00 36.83 C ATOM 1823 O ASN 227 62.386 50.680 −31.379 1.00 36.83 O ATOM 1824 N ALA 228 61.351 48.800 −30.684 1.00 36.83 N ATOM 1825 CA ALA 228 60.015 49.369 −30.717 1.00 36.83 C ATOM 1826 CB ALA 228 59.504 49.429 −32.140 1.00 36.83 C ATOM 1827 C ALA 228 59.042 48.582 −29.853 1.00 36.83 C ATOM 1828 O ALA 228 59.319 47.459 −29.432 1.00 36.83 O ATOM 1829 N LYS 229 57.898 49.195 −29.592 1.00 36.83 N ATOM 1830 CA LYS 229 56.851 48.587 −28.781 1.00 36.83 C ATOM 1831 CB LYS 229 55.955 49.675 −28.161 1.00 36.83 C ATOM 1832 CG LYS 229 54.778 49.139 −27.345 1.00 36.83 C ATOM 1833 CD LYS 229 53.838 50.257 −26.914 1.00 36.83 C ATOM 1834 CE LYS 229 52.808 49.796 −25.876 1.00 36.83 C ATOM 1835 NZ LYS 229 51.706 48.970 −26.416 1.00 36.83 N ATOM 1836 C LYS 229 55.971 47.633 −29.589 1.00 36.83 C ATOM 1837 O LYS 229 55.260 48.048 −30.500 1.00 36.83 O ATOM 1838 N THR 230 56.045 46.351 −29.261 1.00 36.83 N ATOM 1839 CA THR 230 55.198 45.371 −29.916 1.00 36.83 C ATOM 1840 CB THR 230 55.974 44.147 −30.479 1.00 36.83 C ATOM 1841 OG1 THR 230 56.319 43.270 −29.407 1.00 36.83 O ATOM 1842 CG2 THR 230 57.230 44.583 −31.232 1.00 36.83 C ATOM 1843 C THR 230 54.297 44.906 −28.774 1.00 36.83 C ATOM 1844 O THR 230 54.596 45.163 −27.597 1.00 36.83 O ATOM 1845 N THR 231 53.198 44.245 −29.115 1.00 36.83 N ATOM 1846 CA THR 231 52.274 43.757 −28.109 1.00 36.83 C ATOM 1847 CB THR 231 51.043 43.123 −28.763 1.00 36.83 C ATOM 1848 OG1 THR 231 51.466 42.155 −29.728 1.00 36.83 O ATOM 1849 CG2 THR 231 50.210 44.179 −29.452 1.00 36.83 C ATOM 1850 C THR 231 52.949 42.723 −27.213 1.00 36.83 C ATOM 1851 O THR 231 52.448 42.396 −26.147 1.00 36.83 O ATOM 1852 N ARG 232 54.095 42.218 −27.650 1.00 36.83 N ATOM 1853 CA ARG 232 54.830 41.217 −26.885 1.00 36.83 C ATOM 1854 CB ARG 232 55.568 40.283 −27.840 1.00 36.83 C ATOM 1855 CG ARG 232 55.142 38.838 −27.797 1.00 36.83 C ATOM 1856 CD ARG 232 53.793 38.666 −28.409 1.00 36.83 C ATOM 1857 NE ARG 232 53.647 37.359 −29.047 1.00 36.83 N ATOM 1858 CZ ARG 232 53.617 36.200 −28.401 1.00 36.83 C ATOM 1859 NH1 ARG 232 53.726 36.153 −27.083 1.00 36.83 N ATOM 1860 NH2 ARG 232 53.450 35.084 −29.082 1.00 36.83 N ATOM 1861 C ARG 232 55.863 41.795 −25.915 1.00 36.83 C ATOM 1862 O ARG 232 56.250 41.130 −24.952 1.00 36.83 O ATOM 1863 N ASN 233 56.314 43.023 −26.169 1.00 36.83 N ATOM 1864 CA ASN 233 57.355 43.628 −25.344 1.00 36.83 C ATOM 1865 CB ASN 233 58.659 42.842 −25.599 1.00 36.83 C ATOM 1866 CG ASN 233 59.932 43.590 −25.188 1.00 36.83 C ATOM 1867 OD1 ASN 233 59.932 44.454 −24.323 1.00 36.83 O ATOM 1868 ND2 ASN 233 61.037 43.215 −25.810 1.00 36.83 N ATOM 1869 C ASN 233 57.504 45.118 −25.652 1.00 36.83 C ATOM 1870 O ASN 233 57.517 45.524 −26.805 1.00 36.83 O ATOM 1871 N ASN 234 57.606 45.931 −24.610 1.00 36.83 N ATOM 1872 CA ASN 234 57.746 47.373 −24.782 1.00 36.83 C ATOM 1873 CB ASN 234 57.549 48.085 −23.434 1.00 36.83 C ATOM 1874 CG ASN 234 56.139 47.936 −22.900 1.00 36.83 C ATOM 1875 OD1 ASN 234 55.165 48.181 −23.608 1.00 36.83 O ATOM 1876 ND2 ASN 234 56.024 47.534 −21.651 1.00 36.83 N ATOM 1877 C ASN 234 59.085 47.789 −25.404 1.00 36.83 C ATOM 1878 O ASN 234 59.183 48.833 −26.041 1.00 36.83 O ATOM 1879 N ASN 235 60.115 46.974 −25.207 1.00 36.83 N ATOM 1880 CA ASN 235 61.427 47.274 −25.765 1.00 36.83 C ATOM 1881 CB ASN 235 62.441 47.517 −24.637 1.00 36.83 C ATOM 1882 CG ASN 235 63.779 48.018 −25.150 1.00 36.83 C ATOM 1883 OD1 ASN 235 63.834 48.718 −26.141 1.00 36.83 O ATOM 1884 ND2 ASN 235 64.856 47.668 −24.468 1.00 36.83 N ATOM 1885 C ASN 235 61.896 46.142 −26.661 1.00 36.83 C ATOM 1886 O ASN 235 63.017 45.681 −26.538 1.00 36.83 O ATOM 1887 N SER 236 61.031 45.699 −27.571 1.00 36.83 N ATOM 1888 CA SER 236 61.365 44.601 −28.498 1.00 36.83 C ATOM 1889 CB SER 236 60.118 44.129 −29.265 1.00 36.83 C ATOM 1890 OG SER 236 60.476 43.211 −30.291 1.00 36.83 O ATOM 1891 C SER 236 62.453 44.935 −29.517 1.00 36.83 C ATOM 1892 O SER 236 62.424 45.994 −30.147 1.00 36.83 O ATOM 1893 N SER 237 63.411 44.017 −29.665 1.00 36.83 N ATOM 1894 CA SER 237 64.501 44.187 −30.625 1.00 36.83 C ATOM 1895 CB SER 237 65.694 43.301 −30.253 1.00 36.83 C ATOM 1896 OG SER 237 66.144 43.574 −28.949 1.00 36.83 O ATOM 1897 C SER 237 63.987 43.782 −32.011 1.00 36.83 C ATOM 1898 O SER 237 63.618 42.636 −32.226 1.00 36.83 O ATOM 1899 N ARG 238 63.962 44.714 −32.948 1.00 36.83 N ATOM 1900 CA ARG 238 63.465 44.390 −34.271 1.00 36.83 C ATOM 1901 CB ARG 238 62.581 45.521 −34.791 1.00 36.83 C ATOM 1902 CG ARG 238 61.442 45.892 −33.849 1.00 36.83 C ATOM 1903 CD ARG 238 60.704 44.672 −33.290 1.00 36.83 C ATOM 1904 NE ARG 238 59.926 43.945 −34.292 1.00 36.83 N ATOM 1905 CZ ARG 238 59.495 42.696 −34.134 1.00 36.83 C ATOM 1906 NH1 ARG 238 59.767 42.039 −33.012 1.00 36.83 N ATOM 1907 NH2 ARG 238 58.810 42.094 −35.100 1.00 36.83 N ATOM 1908 C ARG 238 64.587 44.076 −35.256 1.00 36.83 C ATOM 1909 O ARG 238 64.389 44.052 −36.465 1.00 36.83 O ATOM 1910 N PHE 239 65.774 43.854 −34.716 1.00 36.83 N ATOM 1911 CA PHE 239 66.939 43.491 −35.501 1.00 36.83 C ATOM 1912 CB PHE 239 67.799 44.709 −35.854 1.00 36.83 C ATOM 1913 CG PHE 239 68.564 45.276 −34.692 1.00 36.83 C ATOM 1914 CD1 PHE 239 67.940 46.099 −33.765 1.00 36.83 C ATOM 1915 CD2 PHE 239 69.906 44.953 −34.506 1.00 36.83 C ATOM 1916 CE1 PHE 239 68.638 46.591 −32.662 1.00 36.83 C ATOM 1917 CE2 PHE 239 70.620 45.435 −33.408 1.00 36.83 C ATOM 1918 CZ PHE 239 69.990 46.252 −32.485 1.00 36.83 C ATOM 1919 C PHE 239 67.727 42.571 −34.592 1.00 36.83 C ATOM 1920 O PHE 239 67.676 42.713 −33.366 1.00 36.83 O ATOM 1921 N GLY 240 68.424 41.614 −35.185 1.00 36.83 N ATOM 1922 CA GLY 240 69.236 40.711 −34.393 1.00 36.83 C ATOM 1923 C GLY 240 70.675 41.163 −34.496 1.00 36.83 C ATOM 1924 O GLY 240 71.033 41.847 −35.445 1.00 36.83 O ATOM 1925 N LYS 241 71.508 40.806 −33.531 1.00 36.83 N ATOM 1926 CA LYS 241 72.894 41.223 −33.599 1.00 36.83 C ATOM 1927 CB LYS 241 73.074 42.624 −32.999 1.00 36.83 C ATOM 1928 CG LYS 241 72.798 42.728 −31.524 1.00 36.83 C ATOM 1929 CD LYS 241 72.990 44.145 −31.022 1.00 36.83 C ATOM 1930 CE LYS 241 72.418 44.302 −29.605 1.00 36.83 C ATOM 1931 NZ LYS 241 72.616 45.681 −29.027 1.00 36.83 N ATOM 1932 C LYS 241 73.865 40.276 −32.937 1.00 36.83 C ATOM 1933 O LYS 241 73.604 39.741 −31.869 1.00 36.83 O ATOM 1934 N PHE 242 74.995 40.072 −33.595 1.00 36.83 N ATOM 1935 CA PHE 242 76.042 39.217 −33.067 1.00 36.83 C ATOM 1936 CB PHE 242 76.597 38.317 −34.160 1.00 36.83 C ATOM 1937 CG PHE 242 77.701 37.412 −33.698 1.00 36.83 C ATOM 1938 CD1 PHE 242 77.465 36.447 −32.719 1.00 36.83 C ATOM 1939 CD2 PHE 242 78.963 37.483 −34.288 1.00 36.83 C ATOM 1940 CE1 PHE 242 78.468 35.558 −32.347 1.00 36.83 C ATOM 1941 CE2 PHE 242 79.970 36.606 −33.924 1.00 36.83 C ATOM 1942 CZ PHE 242 79.726 35.636 −32.955 1.00 36.83 C ATOM 1943 C PHE 242 77.116 40.183 −32.610 1.00 36.83 C ATOM 1944 O PHE 242 77.593 40.995 −33.399 1.00 36.83 O ATOM 1945 N ILE 243 77.473 40.133 −31.333 1.00 36.83 N ATOM 1946 CA ILE 243 78.509 41.034 −30.846 1.00 36.83 C ATOM 1947 CB ILE 243 78.098 41.733 −29.552 1.00 36.83 C ATOM 1948 CG2 ILE 243 79.209 42.628 −29.092 1.00 36.83 C ATOM 1949 CG1 ILE 243 76.827 42.550 −29.768 1.00 36.83 C ATOM 1950 CD1 ILE 243 76.331 43.198 −28.496 1.00 36.83 C ATOM 1951 C ILE 243 79.800 40.285 −30.569 1.00 36.83 C ATOM 1952 O ILE 243 79.784 39.233 −29.939 1.00 36.83 O ATOM 1953 N GLU 244 80.907 40.839 −31.064 1.00 36.83 N ATOM 1954 CA GLU 244 82.243 40.281 −30.861 1.00 36.83 C ATOM 1955 CB GLU 244 83.023 40.186 −32.187 1.00 36.83 C ATOM 1956 CG GLU 244 82.702 38.975 −33.047 1.00 36.83 C ATOM 1957 CD GLU 244 83.697 38.767 −34.186 1.00 36.83 C ATOM 1958 OE1 GLU 244 83.852 39.666 −35.036 1.00 36.83 O ATOM 1959 OE2 GLU 244 84.326 37.691 −34.235 1.00 36.83 O ATOM 1960 C GLU 244 83.031 41.174 −29.907 1.00 36.83 C ATOM 1961 O GLU 244 83.281 42.344 −30.197 1.00 36.83 O ATOM 1962 N ILE 245 83.369 40.636 −28.744 1.00 36.83 N ATOM 1963 CA ILE 245 84.185 41.362 −27.792 1.00 36.83 C ATOM 1964 CB ILE 245 83.835 41.009 −26.339 1.00 36.83 C ATOM 1965 CG2 ILE 245 84.708 41.796 −25.405 1.00 36.83 C ATOM 1966 CG1 ILE 245 82.353 41.296 −26.068 1.00 36.83 C ATOM 1967 CD1 ILE 245 81.975 42.752 −26.160 1.00 36.83 C ATOM 1968 C ILE 245 85.560 40.791 −28.135 1.00 36.83 C ATOM 1969 O ILE 245 85.780 39.574 −28.041 1.00 36.83 O ATOM 1970 N GLN 246 86.470 41.662 −28.562 1.00 36.83 N ATOM 1971 CA GLN 246 87.799 41.229 −28.962 1.00 36.83 C ATOM 1972 CB GLN 246 88.174 41.918 −30.280 1.00 36.83 C ATOM 1973 CG GLN 246 87.235 41.588 −31.420 1.00 36.83 C ATOM 1974 CD GLN 246 87.275 42.618 −32.532 1.00 36.83 C ATOM 1975 OE1 GLN 246 86.682 42.421 −33.598 1.00 36.83 O ATOM 1976 NE2 GLN 246 87.968 43.728 −32.290 1.00 36.83 N ATOM 1977 C GLN 246 88.880 41.471 −27.914 1.00 36.83 C ATOM 1978 O GLN 246 88.979 42.554 −27.338 1.00 36.83 O ATOM 1979 N PHE 247 89.692 40.450 −27.678 1.00 36.83 N ATOM 1980 CA PHE 247 90.766 40.556 −26.708 1.00 36.83 C ATOM 1981 CB PHE 247 90.615 39.509 −25.595 1.00 36.83 C ATOM 1982 CG PHE 247 89.235 39.418 −25.011 1.00 36.83 C ATOM 1983 CD1 PHE 247 88.277 38.575 −25.578 1.00 36.83 C ATOM 1984 CD2 PHE 247 88.888 40.165 −23.895 1.00 36.83 C ATOM 1985 CE1 PHE 247 86.995 38.477 −25.039 1.00 36.83 C ATOM 1986 CE2 PHE 247 87.602 40.073 −23.348 1.00 36.83 C ATOM 1987 CZ PHE 247 86.655 39.224 −23.925 1.00 36.83 C ATOM 1988 C PHE 247 92.115 40.331 −27.375 1.00 36.83 C ATOM 1989 O PHE 247 92.205 39.646 −28.403 1.00 36.83 O ATOM 1990 N ASN 248 93.166 40.894 −26.776 1.00 36.83 N ATOM 1991 CA ASN 248 94.517 40.701 −27.296 1.00 36.83 C ATOM 1992 CB ASN 248 95.436 41.878 −26.924 1.00 36.83 C ATOM 1993 CG ASN 248 95.554 42.097 −25.418 1.00 36.83 C ATOM 1994 OD1 ASN 248 95.658 41.146 −24.642 1.00 36.83 O ATOM 1995 ND2 ASN 248 95.559 43.366 −25.002 1.00 36.83 N ATOM 1996 C ASN 248 95.045 39.397 −26.694 1.00 36.83 C ATOM 1997 O ASN 248 94.352 38.740 −25.916 1.00 36.83 O ATOM 1998 N SER 249 96.272 39.026 −27.051 1.00 36.83 N ATOM 1999 CA SER 249 96.869 37.791 −26.549 1.00 36.83 C ATOM 2000 CB SER 249 98.321 37.662 −27.030 1.00 36.83 C ATOM 2001 OG SER 249 98.434 37.889 −28.428 1.00 36.83 O ATOM 2002 C SER 249 96.849 37.699 −25.031 1.00 36.83 C ATOM 2003 O SER 249 96.725 36.608 −24.477 1.00 36.83 O ATOM 2004 N ALA 250 96.956 38.840 −24.358 1.00 36.83 N ATOM 2005 CA ALA 250 97.003 38.850 −22.901 1.00 36.83 C ATOM 2006 CB ALA 250 97.725 40.084 −22.429 1.00 36.83 C ATOM 2007 C ALA 250 95.667 38.731 −22.174 1.00 36.83 C ATOM 2008 O ALA 250 95.642 38.504 −20.958 1.00 36.83 O ATOM 2009 N GLY 251 94.560 38.902 −22.901 1.00 36.83 N ATOM 2010 CA GLY 251 93.254 38.779 −22.276 1.00 36.83 C ATOM 2011 C GLY 251 92.560 40.101 −22.054 1.00 36.83 C ATOM 2012 O GLY 251 91.461 40.132 −21.511 1.00 36.83 O ATOM 2013 N PHE 252 93.207 41.192 −22.454 1.00 36.83 N ATOM 2014 CA PHE 252 92.620 42.519 −22.312 1.00 36.83 C ATOM 2015 CB PHE 252 93.711 43.592 −22.221 1.00 36.83 C ATOM 2016 CG PHE 252 94.620 43.429 −21.039 1.00 36.83 C ATOM 2017 CD1 PHE 252 94.439 44.196 −19.894 1.00 36.83 C ATOM 2018 CD2 PHE 252 95.644 42.483 −21.061 1.00 36.83 C ATOM 2019 CE1 PHE 252 95.267 44.020 −18.789 1.00 36.83 C ATOM 2020 CE2 PHE 252 96.470 42.301 −19.964 1.00 36.83 C ATOM 2021 CZ PHE 252 96.282 43.068 −18.829 1.00 36.83 C ATOM 2022 C PHE 252 91.748 42.787 −23.529 1.00 36.83 C ATOM 2023 O PHE 252 91.957 42.201 −24.594 1.00 36.83 O ATOM 2024 N ILE 253 90.773 43.675 −23.367 1.00 36.83 N ATOM 2025 CA ILE 253 89.873 44.006 −24.457 1.00 36.83 C ATOM 2026 CB ILE 253 88.538 44.586 −23.930 1.00 36.83 C ATOM 2027 CG2 ILE 253 87.670 45.058 −25.101 1.00 36.83 C ATOM 2028 CG1 ILE 253 87.803 43.520 −23.109 1.00 36.83 C ATOM 2029 CD1 ILE 253 86.541 44.021 −22.446 1.00 36.83 C ATOM 2030 C ILE 253 90.504 45.002 −25.411 1.00 36.83 C ATOM 2031 O ILE 253 90.828 46.126 −25.028 1.00 36.83 O ATOM 2032 N SER 254 90.647 44.583 −26.663 1.00 36.83 N ATOM 2033 CA SER 254 91.244 45.411 −27.697 1.00 36.83 C ATOM 2034 CB SER 254 92.363 44.637 −28.410 1.00 36.83 C ATOM 2035 OG SER 254 91.913 43.381 −28.895 1.00 36.83 O ATOM 2036 C SER 254 90.209 45.869 −28.716 1.00 36.83 C ATOM 2037 O SER 254 90.501 46.730 −29.545 1.00 36.83 O ATOM 2038 N GLY 255 89.009 45.288 −28.659 1.00 36.83 N ATOM 2039 CA GLY 255 87.960 45.682 −29.592 1.00 36.83 C ATOM 2040 C GLY 255 86.578 45.038 −29.460 1.00 36.83 C ATOM 2041 O GLY 255 86.334 44.154 −28.619 1.00 36.83 O ATOM 2042 N ALA 256 85.677 45.507 −30.323 1.00 36.83 N ATOM 2043 CA ALA 256 84.298 45.038 −30.405 1.00 36.83 C ATOM 2044 CB ALA 256 83.436 45.733 −29.364 1.00 36.83 C ATOM 2045 C ALA 256 83.759 45.339 −31.798 1.00 36.83 C ATOM 2046 O ALA 256 83.982 46.426 −32.354 1.00 36.83 O ATOM 2047 N SER 257 83.043 44.370 −32.359 1.00 36.83 N ATOM 2048 CA SER 257 82.446 44.516 −33.673 1.00 36.83 C ATOM 2049 CB SER 257 83.153 43.604 −34.662 1.00 36.83 C ATOM 2050 OG SER 257 82.848 43.994 −35.986 1.00 36.83 O ATOM 2051 C SER 257 80.975 44.128 −33.564 1.00 36.83 C ATOM 2052 O SER 257 80.609 43.281 −32.752 1.00 36.83 O ATOM 2053 N ILE 258 80.128 44.753 −34.367 1.00 36.83 N ATOM 2054 CA ILE 258 78.706 44.445 −34.332 1.00 36.83 C ATOM 2055 CB ILE 258 77.865 45.625 −33.814 1.00 36.83 C ATOM 2056 CG2 ILE 258 76.384 45.231 −33.794 1.00 36.83 C ATOM 2057 CG1 ILE 258 78.310 46.038 −32.420 1.00 36.83 C ATOM 2058 CD1 ILE 258 77.438 47.158 −31.848 1.00 36.83 C ATOM 2059 C ILE 258 78.166 44.120 −35.719 1.00 36.83 C ATOM 2060 O ILE 258 78.346 44.894 −36.656 1.00 36.83 O ATOM 2061 N GLN 259 77.514 42.968 −35.840 1.00 36.83 N ATOM 2062 CA GLN 259 76.883 42.562 −37.093 1.00 36.83 C ATOM 2063 CB GLN 259 77.350 41.164 −37.497 1.00 36.83 C ATOM 2064 CG GLN 259 76.664 40.621 −38.751 1.00 36.83 C ATOM 2065 CD GLN 259 76.888 41.480 −39.991 1.00 36.83 C ATOM 2066 OE1 GLN 259 76.001 41.609 −40.838 1.00 36.83 O ATOM 2067 NE2 GLN 259 78.077 42.058 −40.107 1.00 36.83 N ATOM 2068 C GLN 259 75.358 42.574 −36.871 1.00 36.83 C ATOM 2069 O GLN 259 74.836 41.827 −36.044 1.00 36.83 O ATOM 2070 N SER 260 74.649 43.428 −37.596 1.00 36.83 N ATOM 2071 CA SER 260 73.198 43.526 −37.451 1.00 36.83 C ATOM 2072 CB SER 260 72.732 44.959 −37.676 1.00 36.83 C ATOM 2073 OG SER 260 72.778 45.295 −39.052 1.00 36.83 O ATOM 2074 C SER 260 72.492 42.612 −38.442 1.00 36.83 C ATOM 2075 O SER 260 72.976 42.380 −39.544 1.00 36.83 O ATOM 2076 N TYR 261 71.336 42.101 −38.054 1.00 36.83 N ATOM 2077 CA TYR 261 70.594 41.199 −38.922 1.00 36.83 C ATOM 2078 CB TYR 261 70.710 39.762 −38.409 1.00 36.83 C ATOM 2079 CG TYR 261 72.097 39.175 −38.430 1.00 36.83 C ATOM 2080 CD1 TYR 261 72.682 38.745 −39.619 1.00 36.83 C ATOM 2081 CE1 TYR 261 73.968 38.199 −39.628 1.00 36.83 C ATOM 2082 CD2 TYR 261 72.829 39.044 −37.253 1.00 36.83 C ATOM 2083 CE2 TYR 261 74.113 38.501 −37.253 1.00 36.83 C ATOM 2084 CZ TYR 261 74.672 38.085 −38.436 1.00 36.83 C ATOM 2085 OH TYR 261 75.943 37.582 −38.421 1.00 36.83 O ATOM 2086 C TYR 261 69.108 41.512 −39.039 1.00 36.83 C ATOM 2087 O TYR 261 68.451 41.889 −38.068 1.00 36.83 O ATOM 2088 N LEU 262 68.592 41.341 −40.244 1.00 36.83 N ATOM 2089 CA LEU 262 67.168 41.484 −40.501 1.00 36.83 C ATOM 2090 CB LEU 262 66.496 40.147 −40.156 1.00 36.83 C ATOM 2091 CG LEU 262 65.259 39.696 −40.927 1.00 36.83 C ATOM 2092 CD1 LEU 262 65.663 38.658 −41.979 1.00 36.83 C ATOM 2093 CD2 LEU 262 64.253 39.100 −39.946 1.00 36.83 C ATOM 2094 C LEU 262 66.404 42.605 −39.788 1.00 36.83 C ATOM 2095 O LEU 262 65.498 42.338 −38.994 1.00 36.83 O ATOM 2096 N LEU 263 66.743 43.854 −40.058 1.00 36.83 N ATOM 2097 CA LEU 263 65.991 44.925 −39.428 1.00 36.83 C ATOM 2098 CB LEU 263 66.612 46.291 −39.718 1.00 36.83 C ATOM 2099 CG LEU 263 65.715 47.410 −39.205 1.00 36.83 C ATOM 2100 CD1 LEU 263 65.668 47.333 −37.697 1.00 36.83 C ATOM 2101 CD2 LEU 263 66.232 48.766 −39.668 1.00 36.83 C ATOM 2102 C LEU 263 64.588 44.887 −40.018 1.00 36.83 C ATOM 2103 O LEU 263 64.428 44.790 −41.224 1.00 36.83 O ATOM 2104 N GLU 264 63.573 44.955 −39.167 1.00 36.83 N ATOM 2105 CA GLU 264 62.194 44.949 −39.632 1.00 36.83 C ATOM 2106 CB GLU 264 61.274 44.596 −38.472 1.00 36.83 C ATOM 2107 CG GLU 264 59.791 44.555 −38.808 1.00 36.83 C ATOM 2108 CD GLU 264 58.955 44.705 −37.555 1.00 36.83 C ATOM 2109 OE1 GLU 264 59.221 45.668 −36.819 1.00 36.83 O ATOM 2110 OE2 GLU 264 58.054 43.881 −37.298 1.00 36.83 O ATOM 2111 C GLU 264 61.837 46.334 −40.187 1.00 36.83 C ATOM 2112 O GLU 264 61.182 47.123 −39.520 1.00 36.83 O ATOM 2113 N LYS 265 62.154 46.589 −41.435 1.00 36.83 N ATOM 2114 CA LYS 265 61.975 47.895 −42.034 1.00 36.83 C ATOM 2115 CB LYS 265 62.741 47.989 −43.326 1.00 36.83 C ATOM 2116 CG LYS 265 64.169 47.599 −43.188 1.00 36.83 C ATOM 2117 CD LYS 265 64.965 47.987 −44.361 1.00 36.83 C ATOM 2118 CE LYS 265 64.667 47.160 −45.548 1.00 36.83 C ATOM 2119 NZ LYS 265 65.751 47.201 −46.539 1.00 36.83 N ATOM 2120 C LYS 265 60.537 48.333 −42.235 1.00 36.83 C ATOM 2121 O LYS 265 60.240 49.492 −42.216 1.00 36.83 O ATOM 2122 N SER 266 59.645 47.383 −42.410 1.00 36.83 N ATOM 2123 CA SER 266 58.239 47.686 −42.642 1.00 36.83 C ATOM 2124 CB SER 266 57.476 46.419 −43.010 1.00 36.83 C ATOM 2125 OG SER 266 57.610 45.448 −41.992 1.00 36.83 O ATOM 2126 C SER 266 57.569 48.352 −41.439 1.00 36.83 C ATOM 2127 O SER 266 56.508 48.950 −41.584 1.00 36.83 O ATOM 2128 N ARG 267 58.180 48.251 −40.259 1.00 36.83 N ATOM 2129 CA ARG 267 57.609 48.868 −39.063 1.00 36.83 C ATOM 2130 CB ARG 267 58.393 48.459 −37.807 1.00 36.83 C ATOM 2131 CG ARG 267 57.916 49.149 −36.514 1.00 36.83 C ATOM 2132 CD ARG 267 58.488 48.517 −35.259 1.00 36.83 C ATOM 2133 NE ARG 267 58.051 47.131 −35.082 1.00 36.83 N ATOM 2134 CZ ARG 267 56.839 46.762 −34.691 1.00 36.83 C ATOM 2135 NH1 ARG 267 55.919 47.678 −34.420 1.00 36.83 N ATOM 2136 NH2 ARG 267 56.541 45.476 −34.582 1.00 36.83 N ATOM 2137 C ARG 267 57.579 50.396 −39.172 1.00 36.83 C ATOM 2138 O ARG 267 56.759 51.054 −38.538 1.00 36.83 O ATOM 2139 N VAL 268 58.468 50.952 −39.986 1.00 36.83 N ATOM 2140 CA VAL 268 58.532 52.400 −40.157 1.00 36.83 C ATOM 2141 CB VAL 268 59.759 52.806 −41.019 1.00 36.83 C ATOM 2142 CG1 VAL 268 59.835 54.314 −41.133 1.00 36.83 C ATOM 2143 CG2 VAL 268 61.038 52.243 −40.402 1.00 36.83 C ATOM 2144 C VAL 268 57.267 52.979 −40.800 1.00 36.83 C ATOM 2145 O VAL 268 56.842 54.071 −40.453 1.00 36.83 O ATOM 2146 N VAL 269 56.656 52.228 −41.712 1.00 36.83 N ATOM 2147 CA VAL 269 55.472 52.691 −42.426 1.00 36.83 C ATOM 2148 CB VAL 269 55.608 52.426 −43.961 1.00 36.83 C ATOM 2149 CG1 VAL 269 56.849 53.114 −44.506 1.00 36.83 C ATOM 2150 CG2 VAL 269 55.680 50.924 −44.236 1.00 36.83 C ATOM 2151 C VAL 269 54.166 52.063 −41.946 1.00 36.83 C ATOM 2152 O VAL 269 53.094 52.385 −42.462 1.00 36.83 O ATOM 2153 N PHE 270 54.255 51.172 −40.966 1.00 36.83 N ATOM 2154 CA PHE 270 53.069 50.505 −40.442 1.00 36.83 C ATOM 2155 CB PHE 270 52.572 49.439 −41.423 1.00 36.83 C ATOM 2156 CG PHE 270 51.416 48.629 −40.893 1.00 36.83 C ATOM 2157 CD1 PHE 270 50.129 49.143 −40.905 1.00 36.83 C ATOM 2158 CD2 PHE 270 51.627 47.373 −40.325 1.00 36.83 C ATOM 2159 CE1 PHE 270 49.069 48.428 −40.361 1.00 36.83 C ATOM 2160 CE2 PHE 270 50.573 46.650 −39.778 1.00 36.83 C ATOM 2161 CZ PHE 270 49.294 47.178 −39.796 1.00 36.83 C ATOM 2162 C PHE 270 53.292 49.822 −39.104 1.00 36.83 C ATOM 2163 O PHE 270 54.355 49.240 −38.860 1.00 36.83 O ATOM 2164 N GLN 271 52.276 49.888 −38.248 1.00 36.83 N ATOM 2165 CA GLN 271 52.316 49.229 −36.946 1.00 36.83 C ATOM 2166 CB GLN 271 52.797 50.188 −35.852 1.00 36.83 C ATOM 2167 CG GLN 271 53.994 51.038 −36.264 1.00 36.83 C ATOM 2168 CD GLN 271 53.583 52.297 −37.010 1.00 36.83 C ATOM 2169 OE1 GLN 271 54.329 52.815 −37.841 1.00 36.83 O ATOM 2170 NE2 GLN 271 52.394 52.802 −36.706 1.00 36.83 N ATOM 2171 C GLN 271 50.903 48.758 −36.641 1.00 36.83 C ATOM 2172 O GLN 271 49.949 49.431 −36.976 1.00 36.83 O ATOM 2173 N SER 272 50.773 47.592 −36.024 1.00 36.83 N ATOM 2174 CA SER 272 49.461 47.053 −35.664 1.00 36.83 C ATOM 2175 CB SER 272 49.573 45.565 −35.300 1.00 36.83 C ATOM 2176 OG SER 272 50.080 44.805 −36.387 1.00 36.83 O ATOM 2177 C SER 272 48.911 47.829 −34.459 1.00 36.83 C ATOM 2178 O SER 272 49.634 48.605 −33.825 1.00 36.83 O ATOM 2179 N GLU 273 47.636 47.601 −34.156 1.00 36.83 N ATOM 2180 CA GLU 273 46.940 48.263 −33.046 1.00 36.83 C ATOM 2181 CB GLU 273 45.532 47.665 −32.908 1.00 36.83 C ATOM 2182 CG GLU 273 44.536 48.453 −32.056 1.00 36.83 C ATOM 2183 CD GLU 273 43.111 47.907 −32.179 1.00 36.83 C ATOM 2184 OE1 GLU 273 42.595 47.806 −33.318 1.00 36.83 O ATOM 2185 OE2 GLU 273 42.496 47.577 −31.142 1.00 36.83 O ATOM 2186 C GLU 273 47.701 48.128 −31.735 1.00 36.83 C ATOM 2187 O GLU 273 48.056 47.031 −31.333 1.00 36.83 O ATOM 2188 N THR 274 47.957 49.261 −31.090 1.00 36.83 N ATOM 2189 CA THR 274 48.671 49.343 −29.812 1.00 36.83 C ATOM 2190 CB THR 274 48.199 48.285 −28.785 1.00 36.83 C ATOM 2191 OG1 THR 274 48.752 47.010 −29.130 1.00 36.83 O ATOM 2192 CG2 THR 274 46.685 48.209 −28.746 1.00 36.83 C ATOM 2193 C THR 274 50.207 49.280 −29.843 1.00 36.83 C ATOM 2194 O THR 274 50.840 49.412 −28.805 1.00 36.83 O ATOM 2195 N GLU 275 50.810 49.074 −31.007 1.00 36.83 N ATOM 2196 CA GLU 275 52.269 49.059 −31.080 1.00 36.83 C ATOM 2197 CB GLU 275 52.742 48.028 −32.113 1.00 36.83 C ATOM 2198 CG GLU 275 52.425 46.597 −31.696 1.00 36.83 C ATOM 2199 CD GLU 275 53.033 45.543 −32.597 1.00 36.83 C ATOM 2200 OE1 GLU 275 52.896 44.337 −32.266 1.00 36.83 O ATOM 2201 OE2 GLU 275 53.640 45.917 −33.628 1.00 36.83 O ATOM 2202 C GLU 275 52.764 50.460 −31.448 1.00 36.83 C ATOM 2203 O GLU 275 51.959 51.375 −31.655 1.00 36.83 O ATOM 2204 N ARG 276 54.083 50.626 −31.511 1.00 36.83 N ATOM 2205 CA ARG 276 54.704 51.901 −31.864 1.00 36.83 C ATOM 2206 CB ARG 276 55.388 52.557 −30.662 1.00 36.83 C ATOM 2207 CG ARG 276 54.469 53.023 −29.538 1.00 36.83 C ATOM 2208 CD ARG 276 55.020 54.281 −28.869 1.00 36.83 C ATOM 2209 NE ARG 276 56.454 54.196 −28.597 1.00 36.83 N ATOM 2210 CZ ARG 276 57.138 55.101 −27.908 1.00 36.83 C ATOM 2211 NH1 ARG 276 56.522 56.170 −27.417 1.00 36.83 N ATOM 2212 NH2 ARG 276 58.437 54.941 −27.694 1.00 36.83 N ATOM 2213 C ARG 276 55.765 51.725 −32.936 1.00 36.83 C ATOM 2214 O ARG 276 56.215 50.615 −33.212 1.00 36.83 O ATOM 2215 N ASN 277 56.154 52.842 −33.537 1.00 36.83 N ATOM 2216 CA ASN 277 57.197 52.843 −34.535 1.00 36.83 C ATOM 2217 CB ASN 277 57.156 54.138 −35.343 1.00 36.83 C ATOM 2218 CG ASN 277 57.803 53.999 −36.707 1.00 36.83 C ATOM 2219 OD1 ASN 277 58.907 53.467 −36.834 1.00 36.83 O ATOM 2220 ND2 ASN 277 57.122 54.491 −37.736 1.00 36.83 N ATOM 2221 C ASN 277 58.475 52.783 −33.689 1.00 36.83 C ATOM 2222 O ASN 277 58.399 52.647 −32.472 1.00 36.83 O ATOM 2223 N TYR 278 59.642 52.876 −34.309 1.00 36.83 N ATOM 2224 CA TYR 278 60.877 52.824 −33.528 1.00 36.83 C ATOM 2225 CB TYR 278 62.083 52.795 −34.478 1.00 36.83 C ATOM 2226 CG TYR 278 62.181 51.484 −35.254 1.00 36.83 C ATOM 2227 CD1 TYR 278 62.576 50.301 −34.622 1.00 36.83 C ATOM 2228 CE1 TYR 278 62.620 49.090 −35.315 1.00 36.83 C ATOM 2229 CD2 TYR 278 61.833 51.421 −36.598 1.00 36.83 C ATOM 2230 CE2 TYR 278 61.867 50.234 −37.298 1.00 36.83 C ATOM 2231 CZ TYR 278 62.262 49.067 −36.657 1.00 36.83 C ATOM 2232 OH TYR 278 62.288 47.893 −37.356 1.00 36.83 O ATOM 2233 C TYR 278 60.984 53.977 −32.498 1.00 36.83 C ATOM 2234 O TYR 278 60.582 55.114 −32.759 1.00 36.83 O ATOM 2235 N HIS 279 61.512 53.656 −31.322 1.00 36.83 N ATOM 2236 CA HIS 279 61.673 54.616 −30.243 1.00 36.83 C ATOM 2237 CB HIS 279 62.631 54.082 −29.190 1.00 36.83 C ATOM 2238 CG HIS 279 62.185 52.809 −28.553 1.00 36.83 C ATOM 2239 CD2 HIS 279 62.885 51.723 −28.148 1.00 36.83 C ATOM 2240 ND1 HIS 279 60.871 52.561 −28.219 1.00 36.83 N ATOM 2241 CE1 HIS 279 60.782 51.381 −27.637 1.00 36.83 C ATOM 2242 NE2 HIS 279 61.989 50.853 −27.580 1.00 36.83 N ATOM 2243 C HIS 279 62.167 55.990 −30.686 1.00 36.83 C ATOM 2244 O HIS 279 61.691 57.008 −30.184 1.00 36.83 O ATOM 2245 N ILE 280 63.100 56.019 −31.636 1.00 36.83 N ATOM 2246 CA ILE 280 63.664 57.277 −32.092 1.00 36.83 C ATOM 2247 CB ILE 280 64.693 57.082 −33.206 1.00 36.83 C ATOM 2248 CG2 ILE 280 64.023 56.604 −34.481 1.00 36.83 C ATOM 2249 CG1 ILE 280 65.445 58.403 −33.425 1.00 36.83 C ATOM 2250 CD1 ILE 280 66.289 58.833 −32.216 1.00 36.83 C ATOM 2251 C ILE 280 62.652 58.304 −32.551 1.00 36.83 C ATOM 2252 O ILE 280 62.676 59.441 −32.089 1.00 36.83 O ATOM 2253 N PHE 281 61.744 57.927 −33.440 1.00 36.83 N ATOM 2254 CA PHE 281 60.768 58.899 −33.893 1.00 36.83 C ATOM 2255 CB PHE 281 59.682 58.211 −34.708 1.00 36.83 C ATOM 2256 CG PHE 281 60.164 57.670 −36.013 1.00 36.83 C ATOM 2257 CD1 PHE 281 60.534 58.529 −37.040 1.00 36.83 C ATOM 2258 CD2 PHE 281 60.286 56.299 −36.207 1.00 36.83 C ATOM 2259 CE1 PHE 281 61.022 58.033 −38.238 1.00 36.83 C ATOM 2260 CE2 PHE 281 60.774 55.797 −37.396 1.00 36.83 C ATOM 2261 CZ PHE 281 61.145 56.673 −38.418 1.00 36.83 C ATOM 2262 C PHE 281 60.149 59.653 −32.705 1.00 36.83 C ATOM 2263 O PHE 281 60.016 60.876 −32.745 1.00 36.83 O ATOM 2264 N TYR 282 59.792 58.927 −31.646 1.00 36.83 N ATOM 2265 CA TYR 282 59.180 59.537 −30.466 1.00 36.83 C ATOM 2266 CB TYR 282 58.494 58.464 −29.621 1.00 36.83 C ATOM 2267 CG TYR 282 57.541 57.596 −30.407 1.00 36.83 C ATOM 2268 CD1 TYR 282 57.947 56.364 −30.918 1.00 36.83 C ATOM 2269 CE1 TYR 282 57.072 55.571 −31.688 1.00 36.83 C ATOM 2270 CD2 TYR 282 56.244 58.018 −30.679 1.00 36.83 C ATOM 2271 CE2 TYR 282 55.369 57.237 −31.449 1.00 36.83 C ATOM 2272 CZ TYR 282 55.792 56.017 −31.949 1.00 36.83 C ATOM 2273 OH TYR 282 54.942 55.262 −32.720 1.00 36.83 O ATOM 2274 C TYR 282 60.170 60.331 −29.603 1.00 36.83 C ATOM 2275 O TYR 282 59.827 61.373 −29.042 1.00 36.83 O ATOM 2276 N GLN 283 61.397 59.847 −29.491 1.00 36.83 N ATOM 2277 CA GLN 283 62.388 60.553 −28.697 1.00 36.83 C ATOM 2278 CB GLN 283 63.675 59.744 −28.592 1.00 36.83 C ATOM 2279 CG GLN 283 63.552 58.469 −27.767 1.00 36.83 C ATOM 2280 CD GLN 283 64.834 57.661 −27.777 1.00 36.83 C ATOM 2281 OE1 GLN 283 65.890 58.160 −28.150 1.00 36.83 O ATOM 2282 NE2 GLN 283 64.746 56.409 −27.357 1.00 36.83 N ATOM 2283 C GLN 283 62.686 61.908 −29.313 1.00 36.83 C ATOM 2284 O GLN 283 62.948 62.869 −28.601 1.00 36.83 O ATOM 2285 N LEU 284 62.639 61.986 −30.640 1.00 36.83 N ATOM 2286 CA LEU 284 62.904 63.240 −31.337 1.00 36.83 C ATOM 2287 CB LEU 284 63.120 62.993 −32.837 1.00 36.83 C ATOM 2288 CG LEU 284 63.306 64.235 −33.737 1.00 36.83 C ATOM 2289 CD1 LEU 284 64.711 64.813 −33.582 1.00 36.83 C ATOM 2290 CD2 LEU 284 63.073 63.849 −35.185 1.00 36.83 C ATOM 2291 C LEU 284 61.759 64.237 −31.152 1.00 36.83 C ATOM 2292 O LEU 284 61.977 65.368 −30.720 1.00 36.83 O ATOM 2293 N LEU 285 60.540 63.820 −31.479 1.00 36.83 N ATOM 2294 CA LEU 285 59.398 64.713 −31.367 1.00 36.83 C ATOM 2295 CB LEU 285 58.111 64.011 −31.815 1.00 36.83 C ATOM 2296 CG LEU 285 58.092 63.568 −33.283 1.00 36.83 C ATOM 2297 CD1 LEU 285 56.724 63.044 −33.633 1.00 36.83 C ATOM 2298 CD2 LEU 285 58.459 64.735 −34.188 1.00 36.83 C ATOM 2299 C LEU 285 59.229 65.260 −29.965 1.00 36.83 C ATOM 2300 O LEU 285 58.937 66.444 −29.795 1.00 36.83 O ATOM 2301 N ALA 286 59.433 64.398 −28.972 1.00 36.83 N ATOM 2302 CA ALA 286 59.308 64.742 −27.554 1.00 36.83 C ATOM 2303 CB ALA 286 58.971 63.474 −26.753 1.00 36.83 C ATOM 2304 C ALA 286 60.516 65.427 −26.900 1.00 36.83 C ATOM 2305 O ALA 286 60.355 66.319 −26.078 1.00 36.83 O ATOM 2306 N GLY 287 61.721 64.993 −27.240 1.00 36.83 N ATOM 2307 CA GLY 287 62.903 65.561 −26.617 1.00 36.83 C ATOM 2308 C GLY 287 63.714 66.527 −27.452 1.00 36.83 C ATOM 2309 O GLY 287 64.901 66.730 −27.182 1.00 36.83 O ATOM 2310 N ALA 288 63.092 67.148 −28.445 1.00 36.83 N ATOM 2311 CA ALA 288 63.820 68.085 −29.287 1.00 36.83 C ATOM 2312 CB ALA 288 63.393 67.918 −30.748 1.00 36.83 C ATOM 2313 C ALA 288 63.662 69.548 −28.869 1.00 36.83 C ATOM 2314 O ALA 288 62.552 70.003 −28.571 1.00 36.83 O ATOM 2315 N THR 289 64.781 70.272 −28.862 1.00 36.83 N ATOM 2316 CA THR 289 64.789 71.703 −28.529 1.00 36.83 C ATOM 2317 CB THR 289 66.229 72.255 −28.431 1.00 36.83 C ATOM 2318 OG1 THR 289 66.937 71.947 −29.643 1.00 36.83 O ATOM 2319 CG2 THR 289 66.957 71.657 −27.232 1.00 36.83 C ATOM 2320 C THR 289 64.068 72.482 −29.636 1.00 36.83 C ATOM 2321 O THR 289 64.196 72.155 −30.823 1.00 36.83 O ATOM 2322 N ALA 290 63.343 73.527 −29.250 1.00 36.83 N ATOM 2323 CA ALA 290 62.575 74.338 −30.201 1.00 36.83 C ATOM 2324 CB ALA 290 61.918 75.524 −29.474 1.00 36.83 C ATOM 2325 C ALA 290 63.348 74.839 −31.404 1.00 36.83 C ATOM 2326 O ALA 290 62.764 75.118 −32.457 1.00 36.83 O ATOM 2327 N GLU 291 64.655 74.976 −31.259 1.00 36.83 N ATOM 2328 CA GLU 291 65.477 75.454 −32.371 1.00 36.83 C ATOM 2329 CB GLU 291 66.882 75.835 −31.863 1.00 36.83 C ATOM 2330 CG GLU 291 67.967 75.910 −32.944 1.00 36.83 C ATOM 2331 CD GLU 291 68.514 74.525 −33.318 1.00 36.83 C ATOM 2332 OE1 GLU 291 68.991 73.814 −32.393 1.00 36.83 O ATOM 2333 OE2 GLU 291 68.467 74.155 −34.527 1.00 36.83 O ATOM 2334 C GLU 291 65.546 74.346 −33.417 1.00 36.83 C ATOM 2335 O GLU 291 65.880 74.576 −34.584 1.00 36.83 O ATOM 2336 N GLU 292 65.226 73.133 −32.984 1.00 36.83 N ATOM 2337 CA GLU 292 65.234 71.993 −33.876 1.00 36.83 C ATOM 2338 CB GLU 292 65.797 70.777 −33.134 1.00 36.83 C ATOM 2339 CG GLU 292 67.302 70.934 −32.817 1.00 36.83 C ATOM 2340 CD GLU 292 67.860 69.830 −31.922 1.00 36.83 C ATOM 2341 OE1 GLU 292 67.490 69.783 −30.723 1.00 36.83 O ATOM 2342 OE2 GLU 292 68.676 69.011 −32.422 1.00 36.83 O ATOM 2343 C GLU 292 63.808 71.770 −34.357 1.00 36.83 C ATOM 2344 O GLU 292 63.570 71.583 −35.549 1.00 36.83 O ATOM 2345 N LYS 293 62.852 71.828 −33.438 1.00 36.83 N ATOM 2346 CA LYS 293 61.452 71.638 −33.798 1.00 36.83 C ATOM 2347 CB LYS 293 60.535 72.114 −32.669 1.00 36.83 C ATOM 2348 CG LYS 293 60.592 71.303 −31.379 1.00 36.83 C ATOM 2349 CD LYS 293 59.437 71.698 −30.459 1.00 36.83 C ATOM 2350 CE LYS 293 59.308 70.744 −29.273 1.00 36.83 C ATOM 2351 NZ LYS 293 58.121 71.053 −28.410 1.00 36.83 N ATOM 2352 C LYS 293 61.087 72.395 −35.080 1.00 36.83 C ATOM 2353 O LYS 293 60.699 71.791 −36.076 1.00 36.83 O ATOM 2354 N LYS 294 61.203 73.719 −35.049 1.00 36.83 N ATOM 2355 CA LYS 294 60.879 74.532 −36.216 1.00 36.83 C ATOM 2356 CB LYS 294 60.879 76.027 −35.874 1.00 36.83 C ATOM 2357 CG LYS 294 60.395 76.909 −37.020 1.00 36.83 C ATOM 2358 CD LYS 294 60.809 78.382 −36.846 1.00 36.83 C ATOM 2359 CE LYS 294 59.871 79.301 −37.627 1.00 36.83 C ATOM 2360 NZ LYS 294 59.649 78.857 −39.055 1.00 36.83 N ATOM 2361 C LYS 294 61.859 74.319 −37.361 1.00 36.83 C ATOM 2362 O LYS 294 61.464 74.379 −38.521 1.00 36.83 O ATOM 2363 N ALA 295 63.130 74.088 −37.042 1.00 36.83 N ATOM 2364 CA ALA 295 64.138 73.892 −38.089 1.00 36.83 C ATOM 2365 CB ALA 295 65.531 73.794 −37.472 1.00 36.83 C ATOM 2366 C ALA 295 63.865 72.650 −38.938 1.00 36.83 C ATOM 2367 O ALA 295 64.235 72.604 −40.123 1.00 36.83 O ATOM 2368 N LEU 296 63.225 71.651 −38.323 1.00 36.83 N ATOM 2369 CA LEU 296 62.899 70.400 −39.004 1.00 36.83 C ATOM 2370 CB LEU 296 63.341 69.209 −38.142 1.00 36.83 C ATOM 2371 CG LEU 296 64.832 69.031 −37.823 1.00 36.83 C ATOM 2372 CD1 LEU 296 65.010 68.075 −36.646 1.00 36.83 C ATOM 2373 CD2 LEU 296 65.565 68.511 −39.053 1.00 36.83 C ATOM 2374 C LEU 296 61.397 70.296 −39.310 1.00 36.83 C ATOM 2375 O LEU 296 60.926 69.288 −39.849 1.00 36.83 O ATOM 2376 N HIS 297 60.650 71.342 −38.968 1.00 36.83 N ATOM 2377 CA HIS 297 59.206 71.382 −39.204 1.00 36.83 C ATOM 2378 CB HIS 297 58.903 71.218 −40.692 1.00 36.83 C ATOM 2379 CG HIS 297 59.484 72.297 −41.553 1.00 36.83 C ATOM 2380 CD2 HIS 297 58.893 73.178 −42.391 1.00 36.83 C ATOM 2381 ND1 HIS 297 60.841 72.532 −41.642 1.00 36.83 N ATOM 2382 CE1 HIS 297 61.059 73.509 −42.503 1.00 36.83 C ATOM 2383 NE2 HIS 297 59.893 73.918 −42.972 1.00 36.83 N ATOM 2384 C HIS 297 58.454 70.307 −38.429 1.00 36.83 C ATOM 2385 O HIS 297 57.389 69.847 −38.852 1.00 36.83 O ATOM 2386 N LEU 298 59.013 69.919 −37.291 1.00 36.83 N ATOM 2387 CA LEU 298 58.422 68.891 −36.441 1.00 36.83 C ATOM 2388 CB LEU 298 59.506 68.312 −35.529 1.00 36.83 C ATOM 2389 CG LEU 298 60.638 67.690 −36.356 1.00 36.83 C ATOM 2390 CD1 LEU 298 61.755 67.155 −35.465 1.00 36.83 C ATOM 2391 CD2 LEU 298 60.053 66.579 −37.197 1.00 36.83 C ATOM 2392 C LEU 298 57.243 69.379 −35.607 1.00 36.83 C ATOM 2393 O LEU 298 57.079 70.572 −35.370 1.00 36.83 O ATOM 2394 N ALA 299 56.410 68.443 −35.178 1.00 36.83 N ATOM 2395 CA ALA 299 55.251 68.761 −34.363 1.00 36.83 C ATOM 2396 CB ALA 299 54.070 69.101 −35.246 1.00 36.83 C ATOM 2397 C ALA 299 54.950 67.526 −33.522 1.00 36.83 C ATOM 2398 O ALA 299 55.788 66.634 −33.408 1.00 36.83 O ATOM 2399 N GLY 300 53.751 67.470 −32.946 1.00 36.83 N ATOM 2400 CA GLY 300 53.399 66.328 −32.128 1.00 36.83 C ATOM 2401 C GLY 300 53.343 65.067 −32.964 1.00 36.83 C ATOM 2402 O GLY 300 53.075 65.121 −34.161 1.00 36.83 O ATOM 2403 N PRO 301 53.597 63.906 −32.362 1.00 36.83 N ATOM 2404 CD PRO 301 53.965 63.630 −30.961 1.00 36.83 C ATOM 2405 CA PRO 301 53.545 62.679 −33.147 1.00 36.83 C ATOM 2406 CB PRO 301 53.951 61.606 −32.133 1.00 36.83 C ATOM 2407 CG PRO 301 53.536 62.204 −30.801 1.00 36.83 C ATOM 2408 C PRO 301 52.169 62.445 −33.756 1.00 36.83 C ATOM 2409 O PRO 301 52.052 61.795 −34.795 1.00 36.83 O ATOM 2410 N GUL 302 51.127 62.987 −33.132 1.00 36.83 N ATOM 2411 CA GLU 302 49.761 62.811 −33.648 1.00 36.83 C ATOM 2412 CB GLU 302 48.735 63.389 −32.670 1.00 36.83 C ATOM 2413 CG GLU 302 49.133 64.722 −32.024 1.00 36.83 C ATOM 2414 CD GLU 302 50.092 64.538 −30.846 1.00 36.83 C ATOM 2415 OE1 GLU 302 49.788 63.715 −29.955 1.00 36.83 O ATOM 2416 OE2 GLU 302 51.144 65.213 −30.801 1.00 36.83 O ATOM 2417 C GLU 302 49.517 63.421 −35.029 1.00 36.83 C ATOM 2418 O GLU 302 48.506 63.124 −35.689 1.00 36.83 O ATOM 2419 N SER 303 50.430 64.275 −35.475 1.00 36.83 N ATOM 2420 CA SER 303 50.255 64.904 −36.775 1.00 36.83 C ATOM 2421 CB SER 303 50.776 66.340 −36.729 1.00 36.83 C ATOM 2422 OG SER 303 52.108 66.354 −36.249 1.00 36.83 O ATOM 2423 C SER 303 50.945 64.142 −37.903 1.00 36.83 C ATOM 2424 O SER 303 51.078 64.659 −39.010 1.00 36.83 O ATOM 2425 N PHE 304 51.357 62.907 −37.631 1.00 36.83 N ATOM 2426 CA PHE 304 52.051 62.093 −38.635 1.00 36.83 C ATOM 2427 CB PHE 304 53.521 61.958 −38.231 1.00 36.83 C ATOM 2428 CG PHE 304 54.302 63.249 −38.283 1.00 36.83 C ATOM 2429 CD1 PHE 304 54.803 63.730 −39.490 1.00 36.83 C ATOM 2430 CD2 PHE 304 54.584 63.954 −37.118 1.00 36.83 C ATOM 2431 CE1 PHE 304 55.579 64.889 −39.539 1.00 36.83 C ATOM 2432 CE2 PRE 304 55.363 65.121 −37.158 1.00 36.83 C ATOM 2433 CZ PHE 304 55.860 65.585 −38.370 1.00 36.83 C ATOM 2434 C PHE 304 51.426 60.692 −38.812 1.00 36.83 C ATOM 2435 O PHE 304 51.231 59.958 −37.836 1.00 36.83 O ATOM 2436 N ASN 305 51.127 60.319 −40.054 1.00 36.83 N ATOM 2437 CA ASN 305 50.514 59.021 −40.331 1.00 36.83 C ATOM 2438 CB ASN 305 50.248 58.847 −41.831 1.00 36.83 C ATOM 2439 CG ASN 305 49.445 59.994 −42.420 1.00 36.83 C ATOM 2440 OD1 ASN 305 48.394 60.386 −41.879 1.00 36.83 O ATOM 2441 ND2 ASN 305 49.932 60.544 −43.541 1.00 36.83 N ATOM 2442 C ASN 305 51.341 57.839 −39.836 1.00 36.83 C ATOM 2443 O ASN 305 50.784 56.823 −39.426 1.00 36.83 O ATOM 2444 N TYR 306 52.661 57.967 −39.865 1.00 36.83 N ATOM 2445 CA TYR 306 53.528 56.879 −39.432 1.00 36.83 C ATOM 2446 CB TYR 306 54.954 57.085 −39.957 1.00 36.83 C ATOM 2447 CG TYR 306 55.113 56.883 −41.445 1.00 36.83 C ATOM 2448 CD1 TYR 306 54.268 56.034 −42.155 1.00 36.83 C ATOM 2449 CE1 TYR 306 54.461 55.803 −43.510 1.00 36.83 C ATOM 2450 CD2 TYR 306 56.154 57.498 −42.135 1.00 36.83 C ATOM 2451 CE2 TYR 306 56.357 57.272 −43.491 1.00 36.83 C ATOM 2452 CZ TYR 306 55.511 56.428 −44.168 1.00 36.83 C ATOM 2453 OH TYR 306 55.725 56.220 −45.501 1.00 36.83 O ATOM 2454 C TYR 306 53.579 56.687 −37.920 1.00 36.83 C ATOM 2455 O TYR 306 54.147 55.704 −37.439 1.00 36.83 O ATOM 2456 N LEU 307 52.990 57.617 −37.172 1.00 36.83 N ATOM 2457 CA LEU 307 52.981 57.530 −35.708 1.00 36.83 C ATOM 2458 CB LEU 307 53.896 58.591 −35.111 1.00 36.83 C ATOM 2459 CG LEU 307 55.302 58.719 −35.675 1.00 36.83 C ATOM 2460 CD1 LEU 307 55.890 60.021 −35.204 1.00 36.83 C ATOM 2461 CD2 LEU 307 56.153 57.532 −35.235 1.00 36.83 C ATOM 2462 C LEU 307 51.592 57.726 −35.118 1.00 36.83 C ATOM 2463 O LEU 307 51.414 57.628 −33.906 1.00 36.83 O ATOM 2464 N ASN 308 50.603 58.000 −35.958 1.00 36.83 N ATOM 2465 CA ASN 308 49.261 58.238 −35.443 1.00 36.83 C ATOM 2466 CB ASN 308 48.748 59.598 −35.924 1.00 36.83 C ATOM 2467 CG ASN 308 48.186 59.546 −37.335 1.00 36.83 C ATOM 2468 OD1 ASN 308 48.214 58.509 −38.006 1.00 36.83 O ATOM 2469 ND2 ASN 308 47.666 60.674 −37.793 1.00 36.83 N ATOM 2470 C ASN 308 48.250 57.176 −35.836 1.00 36.83 C ATOM 2471 O ASN 308 47.051 57.431 −35.791 1.00 36.83 O ATOM 2472 N GLN 309 48.716 55.988 −36.206 1.00 36.83 N ATOM 2473 CA GLN 309 47.800 54.938 −36.636 1.00 36.83 C ATOM 2474 CB GLN 309 48.331 54.294 −37.920 1.00 36.83 C ATOM 2475 CG GLN 309 48.234 55.188 −39.150 1.00 36.83 C ATOM 2476 CD GLN 309 46.873 55.080 −39.844 1.00 36.83 C ATOM 2477 OE1 GLN 309 46.565 54.063 −40.484 1.00 36.83 O ATOM 2478 NE2 GLN 309 46.048 56.124 −39.706 1.00 36.83 N ATOM 2479 C GLN 309 47.518 53.858 −35.600 1.00 36.83 C ATOM 2480 O GLN 309 46.398 53.397 −35.478 1.00 36.83 O ATOM 2481 N SER 310 48.537 53.455 −34.857 1.00 36.83 N ATOM 2482 CA SER 310 48.387 52.408 −33.851 1.00 36.83 C ATOM 2483 CB SER 310 49.750 52.077 −33.257 1.00 36.83 C ATOM 2484 OG SER 310 50.281 53.164 −32.526 1.00 36.83 O ATOM 2485 C SER 310 47.414 52.752 −32.722 1.00 36.83 C ATOM 2486 O SER 310 46.718 51.878 −32.206 1.00 36.83 O ATOM 2487 N GLY 311 47.380 54.027 −32.337 1.00 36.83 N ATOM 2488 CA GLY 311 46.494 54.443 −31.271 1.00 36.83 C ATOM 2489 C GLY 311 47.247 54.461 −29.963 1.00 36.83 C ATOM 2490 O GLY 311 46.647 54.511 −28.895 1.00 36.83 O ATOM 2491 N CYS 312 48.571 54.420 −30.064 1.00 36.83 N ATOM 2492 CA CYS 312 49.473 54.426 −28.916 1.00 36.83 C ATOM 2493 CB CYS 312 49.801 52.982 −28.498 1.00 36.83 C ATOM 2494 SG CYS 312 51.259 52.830 −27.427 1.00 36.83 S ATOM 2495 C CYS 312 50.764 55.164 −29.288 1.00 36.83 C ATOM 2496 O CYS 312 51.394 54.837 −30.294 1.00 36.83 O ATOM 2497 N VAL 313 51.148 56.150 −28.475 1.00 36.83 N ATOM 2498 CA VAL 313 52.345 56.943 −28.724 1.00 36.83 C ATOM 2499 CB VAL 313 51.979 58.372 −29.170 1.00 36.83 C ATOM 2500 CG1 VAL 313 51.139 58.318 −30.435 1.00 36.83 C ATOM 2501 CG2 VAL 313 51.233 59.101 −28.049 1.00 36.83 C ATOM 2502 C VAL 313 53.279 57.052 −27.523 1.00 36.83 C ATOM 2503 O VAL 313 54.317 57.711 −27.587 1.00 36.83 O ATOM 2504 N ASP 314 52.917 56.397 −26.429 1.00 36.83 N ATOM 2505 CA ASP 314 53.717 56.452 −25.220 1.00 36.83 C ATOM 2506 CB ASP 314 53.116 57.468 −24.257 1.00 36.83 C ATOM 2507 CG ASP 314 51.633 57.244 −24.056 1.00 36.83 C ATOM 2508 OD1 ASP 314 50.871 57.438 −25.035 1.00 36.83 O ATOM 2509 OD2 ASP 314 51.225 56.854 −22.938 1.00 36.83 O ATOM 2510 C ASP 314 53.741 55.090 −24.555 1.00 36.83 C ATOM 2511 O ASP 314 52.747 54.352 −24.580 1.00 36.83 O ATOM 2512 N ILE 315 54.882 54.781 −23.955 1.00 36.83 N ATOM 2513 CA ILE 315 55.100 53.525 −23.252 1.00 36.83 C ATOM 2514 CB ILE 315 56.488 52.926 −23.606 1.00 36.83 C ATOM 2515 CG2 ILE 315 56.615 51.522 −23.009 1.00 36.83 C ATOM 2516 CG1 ILE 315 56.689 52.888 −25.119 1.00 36.83 C ATOM 2517 CD1 ILE 315 58.058 52.384 −25.524 1.00 36.83 C ATOM 2518 C ILE 315 55.099 53.849 −21.764 1.00 36.83 C ATOM 2519 O ILE 315 55.885 54.682 −21.328 1.00 36.83 O ATOM 2520 N LYS 316 54.241 53.202 −20.977 1.00 36.83 N ATOM 2521 CA LYS 316 54.209 53.480 −19.539 1.00 36.83 C ATOM 2522 CB LYS 316 53.167 52.606 −18.826 1.00 36.83 C ATOM 2523 CG LYS 316 53.143 51.130 −19.197 1.00 36.83 C ATOM 2524 CD LYS 316 52.042 50.397 −18.385 1.00 36.83 C ATOM 2525 CE LYS 316 51.195 49.451 −19.248 1.00 36.83 C ATOM 2526 NZ LYS 316 50.462 50.172 −20.345 1.00 36.83 N ATOM 2527 C LYS 316 55.564 53.312 −18.862 1.00 36.83 C ATOM 2528 O LYS 316 56.279 52.344 −19.125 1.00 36.83 O ATOM 2529 N GLY 317 55.913 54.274 −18.004 1.00 36.83 N ATOM 2530 CA GLY 317 57.175 54.235 −17.277 1.00 36.83 C ATOM 2531 C GLY 317 58.395 54.672 −18.063 1.00 36.83 C ATOM 2532 O GLY 317 59.515 54.677 −17.558 1.00 36.83 O ATOM 2533 N VAL 318 58.186 55.035 −19.314 1.00 36.83 N ATOM 2534 CA VAL 318 59.279 55.465 −20.173 1.00 36.83 C ATOM 2535 CB VAL 318 59.332 54.611 −21.474 1.00 36.83 C ATOM 2536 CG1 VAL 318 60.495 55.038 −22.342 1.00 36.83 C ATOM 2537 CG2 VAL 318 59.449 53.129 −21.118 1.00 36.83 C ATOM 2538 C VAL 318 59.046 56.922 −20.552 1.00 36.83 C ATOM 2539 O VAL 318 57.921 57.313 −20.869 1.00 36.83 O ATOM 2540 N SER 319 60.108 57.716 −20.485 1.00 36.83 N ATOM 2541 CA SER 319 60.043 59.124 −20.857 1.00 36.83 C ATOM 2542 CB SER 319 60.687 59.999 −19.782 1.00 36.83 C ATOM 2543 OG SER 319 61.114 61.218 −20.357 1.00 36.83 O ATOM 2544 C SER 319 60.831 59.249 −22.150 1.00 36.83 C ATOM 2545 O SER 319 62.069 59.242 −22.133 1.00 36.83 O ATOM 2546 N ASP 320 60.120 59.352 −23.267 1.00 36.83 N ATOM 2547 CA ASP 320 60.768 59.449 −24.563 1.00 36.83 C ATOM 2548 CB ASP 320 59.714 59.439 −25.670 1.00 36.83 C ATOM 2549 CG ASP 320 59.071 58.070 −25.838 1.00 36.83 C ATOM 2550 OD1 ASP 320 59.786 57.122 −26.236 1.00 36.83 O ATOM 2551 OD2 ASP 320 57.861 57.934 −25.555 1.00 36.83 O ATOM 2552 C ASP 320 61.670 60.668 −24.674 1.00 36.83 C ATOM 2553 O ASP 320 62.624 60.682 −25.455 1.00 36.83 O ATOM 2554 N SER 321 61.391 61.685 −23.874 1.00 36.83 N ATOM 2555 CA SER 321 62.212 62.892 −23.914 1.00 36.83 C ATOM 2556 CB SER 321 61.448 64.076 −23.336 1.00 36.83 C ATOM 2557 OG SER 321 62.165 65.269 −23.586 1.00 36.83 O ATOM 2558 C SER 321 63.486 62.682 −23.111 1.00 36.83 C ATOM 2559 O SER 321 64.553 63.182 −23.464 1.00 36.83 O ATOM 2560 N GLU 322 63.351 61.931 −22.026 1.00 36.83 N ATOM 2561 CA GLU 322 64.462 61.646 −21.142 1.00 36.83 C ATOM 2562 CB GLU 322 63.917 61.147 −19.791 1.00 36.83 C ATOM 2563 CG GLU 322 64.682 61.632 −18.548 1.00 36.83 C ATOM 2564 CD GLU 322 64.661 63.154 −18.381 1.00 36.83 C ATOM 2565 OE1 GLU 322 63.563 63.717 −18.160 1.00 36.83 O ATOM 2566 OE2 GLU 322 65.744 63.787 −18.472 1.00 36.83 O ATOM 2567 C GLU 322 65.357 60.600 −21.809 1.00 36.83 C ATOM 2568 O GLU 322 66.521 60.432 −21.435 1.00 36.83 O ATOM 2569 N GLU 323 64.809 59.901 −22.800 1.00 36.83 N ATOM 2570 CA GLU 323 65.560 58.874 −23.536 1.00 36.83 C ATOM 2571 CB GLU 323 64.609 57.816 −24.117 1.00 36.83 C ATOM 2572 CG GLU 323 63.797 57.014 −23.097 1.00 36.83 C ATOM 2573 CD GLU 323 64.673 56.249 −22.114 1.00 36.83 C ATOM 2574 OE1 GLU 323 65.742 55.757 −22.537 1.00 36.83 O ATOM 2575 OE2 GLU 323 64.286 56.129 −20.927 1.00 36.83 O ATOM 2576 C GLU 323 66.332 59.542 −24.687 1.00 36.83 C ATOM 2577 O GLU 323 67.449 59.143 −25.020 1.00 36.83 O ATOM 2578 N PHE 324 65.728 60.555 −25.297 1.00 36.83 N ATOM 2579 CA PHE 324 66.390 61.261 −26.387 1.00 36.83 C ATOM 2580 CB PHE 324 65.538 62.427 −26.895 1.00 36.83 C ATOM 2581 CG PHE 324 66.052 63.054 −28.171 1.00 36.83 C ATOM 2582 CD1 PHE 324 66.270 62.280 −29.308 1.00 36.83 C ATOM 2583 CD2 PHE 324 66.268 64.430 −28.251 1.00 36.83 C ATOM 2584 CE1 PHE 324 66.691 62.862 −30.506 1.00 36.83 C ATOM 2585 CE2 PHE 324 66.689 65.029 −29.440 1.00 36.83 C ATOM 2586 CZ PHE 324 66.901 64.242 −30.576 1.00 36.83 C ATOM 2587 C PHE 324 67.719 61.787 −25.869 1.00 36.83 C ATOM 2588 O PHE 324 68.714 61.770 −26.595 1.00 36.83 O ATOM 2589 N LYS 325 67.733 62.241 −24.613 1.00 36.83 N ATOM 2590 CA LYS 325 68.960 62.760 −24.013 1.00 36.83 C ATOM 2591 CB LYS 325 68.702 63.284 −22.593 1.00 36.83 C ATOM 2592 CG LYS 325 67.635 64.371 −22.521 1.00 36.83 C ATOM 2593 CD LYS 325 67.416 64.868 −21.087 1.00 36.83 C ATOM 2594 CE LYS 325 66.436 66.032 −21.022 1.00 36.83 C ATOM 2595 NZ LYS 325 65.057 65.697 −21.497 1.00 36.83 N ATOM 2596 C LYS 325 70.005 61.651 −23.977 1.00 36.83 C ATOM 2597 O LYS 325 71.144 61.844 −24.420 1.00 36.83 O ATOM 2598 N ILE 326 69.620 60.485 −23.460 1.00 36.83 N ATOM 2599 CA ILE 326 70.547 59.358 −23.392 1.00 36.83 C ATOM 2600 CB ILE 326 69.869 58.060 −22.880 1.00 36.83 C ATOM 2601 CG2 ILE 326 70.861 56.922 −22.925 1.00 36.83 C ATOM 2602 CG1 ILE 326 69.359 58.239 −21.450 1.00 36.83 C ATOM 2603 CD1 ILE 326 70.438 58.632 −20.452 1.00 36.83 C ATOM 2604 C ILE 326 71.100 59.045 −24.772 1.00 36.83 C ATOM 2605 O ILE 326 72.295 58.799 −24.931 1.00 36.83 O ATOM 2606 N THR 327 70.228 59.047 −25.774 1.00 36.83 N ATOM 2607 CA THR 327 70.656 58.726 −27.130 1.00 36.83 C ATOM 2608 CB THR 327 69.454 58.692 −28.092 1.00 36.83 C ATOM 2609 OG1 THR 327 68.479 57.761 −27.600 1.00 36.83 O ATOM 2610 CG2 THR 327 69.892 58.260 −29.480 1.00 36.83 C ATOM 2611 C THR 327 71.717 59.693 −27.654 1.00 36.83 C ATOM 2612 O THR 327 72.696 59.258 −28.256 1.00 36.83 O ATOM 2613 N ARG 328 71.536 60.991 −27.405 1.00 36.83 N ATOM 2614 CA ARG 328 72.490 62.012 −27.863 1.00 36.83 C ATOM 2615 CB ARG 328 71.889 63.410 −27.697 1.00 36.83 C ATOM 2616 CG ARG 328 70.519 63.564 −28.347 1.00 36.83 C ATOM 2617 CD ARG 328 69.993 65.013 −28.324 1.00 36.83 C ATOM 2618 NE ARG 328 70.731 65.893 −29.233 1.00 36.83 N ATOM 2619 CZ ARG 328 70.272 67.064 −29.689 1.00 36.83 C ATOM 2620 NH1 ARG 328 69.066 67.504 −29.317 1.00 36.83 N ATOM 2621 NH2 ARG 328 71.017 67.791 −30.530 1.00 36.83 N ATOM 2622 C ARG 328 73.822 61.933 −27.113 1.00 36.83 C ATOM 2623 O ARG 328 74.894 62.120 −27.696 1.00 36.83 O ATOM 2624 N GLN 329 73.756 61.649 −25.815 1.00 36.83 N ATOM 2625 CA GLN 329 74.961 61.529 −25.015 1.00 36.83 C ATOM 2626 CB GLN 329 74.597 61.422 −23.537 1.00 36.83 C ATOM 2627 CG GLN 329 75.722 61.830 −22.619 1.00 36.83 C ATOM 2628 CD GLN 329 75.212 62.588 −21.407 1.00 36.83 C ATOM 2629 OE1 GLN 329 74.343 63.467 −21.528 1.00 36.83 O ATOM 2630 NE2 GLN 329 75.747 62.262 −20.233 1.00 36.83 N ATOM 2631 C GLN 329 75.673 60.265 −25.483 1.00 36.83 C ATOM 2632 O GLN 329 76.912 60.162 −25.453 1.00 36.83 O ATOM 2633 N ALA 330 74.878 59.302 −25.931 1.00 36.83 N ATOM 2634 CA ALA 330 75.433 58.054 −26.432 1.00 36.83 C ATOM 2635 CB ALA 330 74.307 57.045 −26.705 1.00 36.83 C ATOM 2636 C ALA 330 76.181 58.384 −27.721 1.00 36.83 C ATOM 2637 O ALA 330 77.337 57.998 −27.913 1.00 36.83 O ATOM 2638 N MET 331 75.508 59.116 −28.599 1.00 36.83 N ATOM 2639 CA MET 331 76.115 59.505 −29.855 1.00 36.83 C ATOM 2640 CB MET 331 75.104 60.284 −30.686 1.00 36.83 C ATOM 2641 CG MET 331 73.870 59.457 −30.982 1.00 36.83 C ATOM 2642 SD MET 331 72.760 60.204 −32.154 1.00 36.83 S ATOM 2643 CE MET 331 72.865 59.068 −33.498 1.00 36.83 C ATOM 2644 C MET 331 77.397 60.320 −29.634 1.00 36.83 C ATOM 2645 O MET 331 78.333 60.209 −30.418 1.00 36.83 O ATOM 2646 N ASP 332 77.452 61.119 −28.564 1.00 36.83 N ATOM 2647 CA ASP 332 78.659 61.912 −28.275 1.00 36.83 C ATOM 2648 CB ASP 332 78.438 62.875 −27.096 1.00 36.83 C ATOM 2649 CG ASP 332 77.561 64.049 −27.448 1.00 36.83 C ATOM 2650 OD1 ASP 332 77.709 64.596 −28.563 1.00 36.83 O ATOM 2651 OD2 ASP 332 76.730 64.442 −26.597 1.00 36.83 O ATOM 2652 C ASP 332 79.863 61.030 −27.919 1.00 36.83 C ATOM 2653 O ASP 332 80.932 61.158 −28.515 1.00 36.83 O ATOM 2654 N ILE 333 79.698 60.151 −26.935 1.00 36.83 N ATOM 2655 CA ILE 333 80.801 59.306 −26.513 1.00 36.83 C ATOM 2656 CB ILE 333 80.406 58.434 −25.302 1.00 36.83 C ATOM 2657 CG2 ILE 333 81.511 57.432 −24.998 1.00 36.83 C ATOM 2658 CG1 ILE 333 80.194 59.326 −24.076 1.00 36.83 C ATOM 2659 CD1 ILE 333 78.785 59.356 −23.557 1.00 36.83 C ATOM 2660 C ILE 333 81.330 58.418 −27.637 1.00 36.83 C ATOM 2661 O ILE 333 82.539 58.153 −27.723 1.00 36.83 O ATOM 2662 N VAL 334 80.433 57.954 −28.500 1.00 36.83 N ATOM 2663 CA VAL 334 80.861 57.113 −29.601 1.00 36.83 C ATOM 2664 CB VAL 334 79.637 56.528 −30.381 1.00 36.83 C ATOM 2665 CG1 VAL 334 80.088 55.915 −31.704 1.00 36.83 C ATOM 2666 CG2 VAL 334 78.967 55.442 −29.528 1.00 36.83 C ATOM 2667 C VAL 334 81.771 57.919 −30.529 1.00 36.83 C ATOM 2668 O VAL 334 82.854 57.465 −30.890 1.00 36.83 O ATOM 2669 N GLY 335 81.344 59.118 −30.909 1.00 36.83 N ATOM 2670 CA GLY 335 82.187 59.923 −31.772 1.00 36.83 C ATOM 2671 C GLY 335 81.451 60.483 −32.960 1.00 36.83 C ATOM 2672 O GLY 335 82.057 60.842 −33.961 1.00 36.83 O ATOM 2673 N PHE 336 80.130 60.535 −32.864 1.00 36.83 N ATOM 2674 CA PHE 336 79.336 61.086 −33.959 1.00 36.83 C ATOM 2675 CB PHE 336 77.886 60.621 −33.875 1.00 36.83 C ATOM 2676 CG PHE 336 77.672 59.226 −34.370 1.00 36.83 C ATOM 2677 CD1 PHE 336 78.063 58.134 −33.609 1.00 36.83 C ATOM 2678 CD2 PHE 336 77.079 59.001 −35.611 1.00 36.83 C ATOM 2679 CE1 PHE 336 77.858 56.828 −34.081 1.00 36.83 C ATOM 2680 CE2 PHE 336 76.873 57.695 −36.086 1.00 36.83 C ATOM 2681 CZ PHE 336 77.260 56.617 −35.323 1.00 36.83 C ATOM 2682 C PHE 336 79.390 62.589 −33.841 1.00 36.83 C ATOM 2683 O PHE 336 78.973 63.146 −32.825 1.00 36.83 O ATOM 2684 N SER 337 79.909 63.235 −34.879 1.00 36.83 N ATOM 2685 CA SER 337 80.037 64.694 −34.922 1.00 36.83 C ATOM 2686 CB SER 337 80.532 65.140 −36.298 1.00 36.83 C ATOM 2687 OG SER 337 79.497 65.015 −37.268 1.00 36.83 O ATOM 2688 C SER 337 78.699 65.362 −34.654 1.00 36.83 C ATOM 2689 O SER 337 77.677 64.690 −34.496 1.00 36.83 O ATOM 2690 N GLN 338 78.709 66.689 −34.599 1.00 36.83 N ATOM 2691 CA GLN 338 77.487 67.452 −34.366 1.00 36.83 C ATOM 2692 CB GLN 338 77.810 68.829 −33.758 1.00 36.83 C ATOM 2693 CG GLN 338 78.568 68.836 −32.420 1.00 36.83 C ATOM 2694 CD GLN 338 80.093 68.722 −32.564 1.00 36.83 C ATOM 2695 OE1 GLN 338 80.835 69.062 −31.637 1.00 36.83 O ATOM 2696 NE2 GLN 338 80.560 68.235 −33.715 1.00 36.83 N ATOM 2697 C GLN 338 76.845 67.664 −35.738 1.00 36.83 C ATOM 2698 O GLN 338 75.671 68.028 −35.861 1.00 36.83 O ATOM 2699 N GLU 339 77.645 67.443 −36.774 1.00 36.83 N ATOM 2700 CA GLU 339 77.190 67.621 −38.142 1.00 36.83 C ATOM 2701 CB GLU 339 78.397 67.952 −39.038 1.00 36.83 C ATOM 2702 CG GLU 339 78.063 68.640 −40.367 1.00 36.83 C ATOM 2703 CD GLU 339 78.985 69.836 −40.655 1.00 36.83 C ATOM 2704 OE1 GLU 339 78.944 70.400 −41.779 1.00 36.83 O ATOM 2705 OE2 GLU 339 79.749 70.215 −39.740 1.00 36.83 O ATOM 2706 C GLU 339 76.506 66.326 −38.583 1.00 36.83 C ATOM 2707 O GLU 339 75.641 66.318 −39.462 1.00 36.83 O ATOM 2708 N GLU 340 76.896 65.230 −37.956 1.00 36.83 N ATOM 2709 CA GLU 340 76.312 63.940 −38.286 1.00 36.83 C ATOM 2710 CB GLU 340 77.294 62.834 −37.916 1.00 36.83 C ATOM 2711 CG GLU 340 78.328 62.653 −38.991 1.00 36.83 C ATOM 2712 CD GLU 340 79.621 62.045 −38.504 1.00 36.83 C ATOM 2713 OE1 GLU 340 80.410 61.611 −39.360 1.00 36.83 O ATOM 2714 OE2 GLU 340 79.866 62.014 −37.281 1.00 36.83 O ATOM 2715 C GLU 340 74.966 63.763 −37.590 1.00 36.83 C ATOM 2716 O GLU 340 73.947 63.533 −38.244 1.00 36.83 O ATOM 2717 N GLN 341 74.960 63.907 −36.270 1.00 36.83 N ATOM 2718 CA GLN 341 73.729 63.772 −35.507 1.00 36.83 C ATOM 2719 CB GLN 341 73.953 64.204 −34.054 1.00 36.83 C ATOM 2720 CG GLN 341 75.127 63.498 −33.415 1.00 36.83 C ATOM 2721 CD GLN 341 75.323 63.838 −31.950 1.00 36.83 C ATOM 2722 OE1 GLN 341 76.389 63.561 −31.379 1.00 36.83 O ATOM 2723 NE2 GLN 341 74.301 64.432 −31.326 1.00 36.83 N ATOM 2724 C GLN 341 72.649 64.622 −36.160 1.00 36.83 C ATOM 2725 O GLN 341 71.537 64.144 −36.403 1.00 36.83 O ATOM 2726 N MET 342 72.985 65.871 −36.476 1.00 36.83 N ATOM 2727 CA MET 342 72.014 66.762 −37.107 1.00 36.83 C ATOM 2728 CB MET 342 72.661 68.104 −37.463 1.00 36.83 C ATOM 2729 CG MET 342 71.731 69.064 −38.179 1.00 36.83 C ATOM 2730 SD MET 342 70.128 69.201 −37.374 1.00 36.83 S ATOM 2731 CE MET 342 70.616 69.963 −35.783 1.00 36.83 C ATOM 2732 C MET 342 71.436 66.135 −38.356 1.00 36.83 C ATOM 2733 O MET 342 70.238 66.217 −38.590 1.00 36.83 O ATOM 2734 N SER 343 72.288 65.509 −39.162 1.00 36.83 N ATOM 2735 CA SER 343 71.835 64.860 −40.391 1.00 36.83 C ATOM 2736 CB SER 343 73.034 64.329 −41.180 1.00 36.83 C ATOM 2737 OG SER 343 74.061 65.296 −41.300 1.00 36.83 O ATOM 2738 C SER 343 70.915 63.688 −40.022 1.00 36.83 C ATOM 2739 O SER 343 69.845 63.492 −40.617 1.00 36.83 O ATOM 2740 N ILE 344 71.345 62.914 −39.029 1.00 36.83 N ATOM 2741 CA ILE 344 70.574 61.772 −38.561 1.00 36.83 C ATOM 2742 CB ILE 344 71.240 61.160 −37.318 1.00 36.83 C ATOM 2743 CG2 ILE 344 70.362 60.039 −36.751 1.00 36.83 C ATOM 2744 CG1 ILE 344 72.639 60.655 −37.708 1.00 36.83 C ATOM 2745 CD1 ILE 344 73.476 60.053 −36.578 1.00 36.83 C ATOM 2746 C ILE 344 69.144 62.215 −38.235 1.00 36.83 C ATOM 2747 O ILE 344 68.178 61.568 −38.632 1.00 36.83 O ATOM 2748 N PHE 345 69.002 63.336 −37.536 1.00 36.83 N ATOM 2749 CA PHE 345 67.671 63.816 −37.201 1.00 36.83 C ATOM 2750 CB PHE 345 67.740 64.804 −36.031 1.00 36.83 C ATOM 2751 CG PHE 345 68.439 64.247 −34.827 1.00 36.83 C ATOM 2752 CD1 PHE 345 68.447 62.874 −34.587 1.00 36.83 C ATOM 2753 CD2 PHE 345 69.099 65.082 −33.937 1.00 36.83 C ATOM 2754 CE1 PHE 345 69.101 62.337 −33.486 1.00 36.83 C ATOM 2755 CE2 PHE 345 69.760 64.557 −32.822 1.00 36.83 C ATOM 2756 CZ PHE 345 69.761 63.177 −32.597 1.00 36.83 C ATOM 2757 C PHE 345 66.932 64.412 −38.396 1.00 36.83 C ATOM 2758 O PHE 345 65.704 64.347 −38.452 1.00 36.83 O ATOM 2759 N LYS 346 67.662 64.977 −39.357 1.00 36.83 N ATOM 2760 CA LYS 346 67.015 65.525 −40.552 1.00 36.83 C ATOM 2761 CB LYS 346 68.021 66.235 −41.458 1.00 36.83 C ATOM 2762 CG LYS 346 68.595 67.541 −40.913 1.00 36.83 C ATOM 2763 CD LYS 346 69.757 68.004 −41.779 1.00 36.83 C ATOM 2764 CE LYS 346 70.461 69.224 −41.185 1.00 36.83 C ATOM 2765 NZ LYS 346 71.799 69.497 −41.817 1.00 36.83 N ATOM 2766 C LYS 346 66.427 64.335 −41.309 1.00 36.83 C ATOM 2767 O LYS 346 65.339 64.418 −41.886 1.00 36.83 O ATOM 2768 N ILE 347 67.149 63.219 −41.308 1.00 36.83 N ATOM 2769 CA ILE 347 66.650 62.041 −41.991 1.00 36.83 C ATOM 2770 CB ILE 347 67.714 60.929 −42.087 1.00 36.83 C ATOM 2771 CG2 ILE 347 67.066 59.643 −42.586 1.00 36.83 C ATOM 2772 CG1 ILE 347 68.803 61.338 −43.070 1.00 36.83 C ATOM 2773 CD1 ILE 347 70.019 60.443 −43.050 1.00 36.83 C ATOM 2774 C ILE 347 65.416 61.506 −41.281 1.00 36.83 C ATOM 2775 O ILE 347 64.438 61.164 −41.928 1.00 36.83 O ATOM 2776 N ILE 348 65.464 61.448 −39.953 1.00 36.83 N ATOM 2777 CA ILE 348 64.337 60.953 −39.171 1.00 36.83 C ATOM 2778 CB ILE 348 64.643 60.968 −37.658 1.00 36.83 C ATOM 2779 CG2 ILE 348 63.427 60.524 −36.880 1.00 36.83 C ATOM 2780 CG1 ILE 348 65.858 60.091 −37.358 1.00 36.83 C ATOM 2781 CD1 ILE 348 65.715 58.627 −37.735 1.00 36.83 C ATOM 2782 C ILE 348 63.111 61.822 −39.451 1.00 36.83 C ATOM 2783 O ILE 348 62.048 61.306 −39.763 1.00 36.83 O ATOM 2784 N ALA 349 63.261 63.140 −39.354 1.00 36.83 N ATOM 2785 CA ALA 349 62.141 64.038 −39.632 1.00 36.83 C ATOM 2786 CB ALA 349 62.548 65.460 −39.368 1.00 36.83 C ATOM 2787 C ALA 349 61.662 63.883 −41.084 1.00 36.83 C ATOM 2788 O ALA 349 60.448 63.860 −41.357 1.00 36.83 O ATOM 2789 N GLY 350 62.617 63.763 −42.008 1.00 36.83 N ATOM 2790 CA GLY 350 62.279 63.608 −43.417 1.00 36.83 C ATOM 2791 C GLY 350 61.397 62.404 −43.680 1.00 36.83 C ATOM 2792 O GLY 350 60.445 62.455 −44.468 1.00 36.83 O ATOM 2793 N ILE 351 61.724 61.304 −43.018 1.00 36.83 N ATOM 2794 CA ILE 351 60.950 60.083 −43.156 1.00 36.83 C ATOM 2795 CB ILE 351 61.549 58.983 −42.260 1.00 36.83 C ATOM 2796 CG2 ILE 351 60.572 57.850 −42.087 1.00 36.83 C ATOM 2797 CG1 ILE 351 62.888 58.532 −42.860 1.00 36.83 C ATOM 2798 CD1 ILE 351 63.558 57.412 −42.150 1.00 36.83 C ATOM 2799 C ILE 351 59.510 60.371 −42.749 1.00 36.83 C ATOM 2800 O ILE 351 58.557 59.956 −43.424 1.00 36.83 O ATOM 2801 N LEU 352 59.355 61.095 −41.645 1.00 36.83 N ATOM 2802 CA LEU 352 58.035 61.431 −41.143 1.00 36.83 C ATOM 2803 CB LEU 352 58.155 62.144 −39.794 1.00 36.83 C ATOM 2804 CG LEU 352 58.642 61.248 −38.639 1.00 36.83 C ATOM 2805 CD1 LEU 352 58.857 62.076 −37.391 1.00 36.83 C ATOM 2806 CD2 LEU 352 57.628 60.173 −38.365 1.00 36.83 C ATOM 2807 C LEU 352 57.246 62.278 −42.142 1.00 36.83 C ATOM 2808 O LEU 352 56.070 62.004 −42.403 1.00 36.83 O ATOM 2809 N HIS 353 57.886 63.289 −42.720 1.00 36.83 N ATOM 2810 CA HIS 353 57.202 64.133 −43.694 1.00 36.83 C ATOM 2811 CB HIS 353 58.098 65.305 −44.104 1.00 36.83 C ATOM 2812 CG HIS 353 58.373 66.263 −42.987 1.00 36.83 C ATOM 2813 CD2 HIS 353 59.519 66.568 −42.331 1.00 36.83 C ATOM 2814 ND1 HIS 353 57.380 67.002 −42.381 1.00 36.83 N ATOM 2815 CE1 HIS 353 57.900 67.719 −41.401 1.00 36.83 C ATOM 2816 NE2 HIS 353 59.197 67.472 −41.351 1.00 36.83 N ATOM 2817 C HIS 353 56.745 63.346 −44.924 1.00 36.83 C ATOM 2818 O HIS 353 55.627 63.541 −45.403 1.00 36.83 O ATOM 2819 N LEU 354 57.587 62.440 −45.419 1.00 36.83 N ATOM 2820 CA LEU 354 57.216 61.658 −46.590 1.00 36.83 C ATOM 2821 CB LEU 354 58.335 60.683 −46.973 1.00 36.83 C ATOM 2822 CG LEU 354 59.589 61.338 −47.556 1.00 36.83 C ATOM 2823 CD1 LEU 354 60.680 60.293 −47.749 1.00 36.83 C ATOM 2824 CD2 LEU 354 59.237 62.032 −48.867 1.00 36.83 C ATOM 2825 C LEU 354 55.937 60.885 −46.325 1.00 36.83 C ATOM 2826 O LEU 354 55.107 60.706 −47.223 1.00 36.83 O ATOM 2827 N GLY 355 55.789 60.431 −45.084 1.00 36.83 N ATOM 2828 CA GLY 355 54.616 59.674 −44.711 1.00 36.83 C ATOM 2829 C GLY 355 53.328 60.472 −44.794 1.00 36.83 C ATOM 2830 O GLY 355 52.243 59.887 −44.918 1.00 36.83 O ATOM 2831 N ASN 356 53.441 61.800 −44.735 1.00 36.83 N ATOM 2832 CA ASN 356 52.263 62.657 −44.788 1.00 36.83 C ATOM 2833 CB ASN 356 52.478 63.924 −43.937 1.00 36.83 C ATOM 2834 CG ASN 356 52.393 63.638 −42.444 1.00 36.83 C ATOM 2835 OD1 ASN 356 52.444 64.546 −41.614 1.00 36.83 O ATOM 2836 ND2 ASN 356 52.262 62.361 −42.098 1.00 36.83 N ATOM 2837 C ASN 356 51.846 63.031 −46.201 1.00 36.83 C ATOM 2838 O ASN 356 50.727 63.500 −46.410 1.00 36.83 O ATOM 2839 N ILE 357 52.742 62.832 −47.170 1.00 36.83 N ATOM 2840 CA ILE 357 52.419 63.128 −48.564 1.00 36.83 C ATOM 2841 CB ILE 357 53.517 62.615 −49.516 1.00 36.83 C ATOM 2842 CG2 ILE 357 53.021 62.688 −50.966 1.00 36.83 C ATOM 2843 CG1 ILE 357 54.802 63.417 −49.305 1.00 36.83 C ATOM 2844 CD1 ILE 357 55.929 62.989 −50.176 1.00 36.83 C ATOM 2845 C ILE 357 51.117 62.398 −48.881 1.00 36.83 C ATOM 2846 O ILE 357 51.002 61.201 −48.616 1.00 36.83 O ATOM 2847 N LYS 358 50.152 63.104 −49.462 1.00 36.83 N ATOM 2848 CA LYS 358 48.851 62.511 −49.757 1.00 36.83 C ATOM 2849 CB LYS 358 47.771 63.271 −48.964 1.00 36.83 C ATOM 2850 CG LYS 358 46.562 62.436 −48.590 1.00 36.83 C ATOM 2851 CD LYS 358 45.283 62.900 −49.274 1.00 36.83 C ATOM 2852 CE LYS 358 44.719 64.175 −48.667 1.00 36.83 C ATOM 2853 NZ LYS 358 45.468 65.431 −49.032 1.00 36.83 N ATOM 2854 C LYS 358 48.451 62.437 −51.246 1.00 36.83 C ATOM 2855 O LYS 358 47.733 63.299 −51.754 1.00 36.83 O ATOM 2856 N PHE 359 48.899 61.396 −51.941 1.00 36.83 N ATOM 2857 CA PHE 359 48.551 61.225 −53.346 1.00 36.83 C ATOM 2858 CB PHE 359 49.230 59.969 −53.913 1.00 36.83 C ATOM 2859 CG PHE 359 50.708 59.905 −53.664 1.00 36.83 C ATOM 2860 CD1 PHE 359 51.579 60.770 −54.320 1.00 36.83 C ATOM 2861 CD2 PHE 359 51.233 58.981 −52.760 1.00 36.83 C ATOM 2862 CE1 PHE 359 52.942 60.721 −54.081 1.00 36.83 C ATOM 2863 CE2 PHE 359 52.608 58.923 −52.514 1.00 36.83 C ATOM 2864 CZ PHE 359 53.459 59.794 −53.175 1.00 36.83 C ATOM 2865 C PHE 359 47.028 61.059 −53.465 1.00 36.83 C ATOM 2866 O PHE 359 46.354 60.744 −52.492 1.00 36.83 O ATOM 2867 N GLU 360 46.496 61.270 −54.664 1.00 36.83 N ATOM 2868 CA GLU 360 45.071 61.112 −54.925 1.00 36.83 C ATOM 2869 CB GLU 360 44.269 62.259 −54.289 1.00 36.83 C ATOM 2870 CG GLU 360 44.833 63.638 −54.558 1.00 36.83 C ATOM 2871 CD GLU 360 44.812 64.526 −53.323 1.00 36.83 C ATOM 2872 OE1 GLU 360 45.732 65.382 −53.212 1.00 36.83 O ATOM 2873 OE2 GLU 360 43.888 64.375 −52.475 1.00 36.83 O ATOM 2874 C GLU 360 44.871 61.072 −56.432 1.00 36.83 C ATOM 2875 O GLU 360 45.683 61.622 −57.188 1.00 36.83 O ATOM 2876 N LYS 361 43.810 60.398 −56.866 1.00 36.83 N ATOM 2877 CA LYS 361 43.513 60.263 −58.282 1.00 36.83 C ATOM 2878 CB LYS 361 42.250 59.423 −58.471 1.00 36.83 C ATOM 2879 CG LYS 361 42.072 58.835 −59.866 1.00 36.83 C ATOM 2880 CD LYS 361 41.018 57.731 −59.830 1.00 36.83 C ATOM 2881 CE LYS 361 40.850 57.064 −61.185 1.00 36.83 C ATOM 2882 NZ LYS 361 40.401 58.049 −62.232 1.00 36.83 N ATOM 2883 C LYS 361 43.323 61.631 −58.908 1.00 36.83 C ATOM 2884 O LYS 361 42.796 62.534 −58.269 1.00 36.83 O ATOM 2885 N GLY 362 43.760 61.788 −60.153 1.00 36.83 N ATOM 2886 CA GLY 362 43.621 63.072 −60.829 1.00 36.83 C ATOM 2887 C GLY 362 42.649 62.935 −61.979 1.00 36.83 C ATOM 2888 O GLY 362 41.577 62.349 −61.817 1.00 36.83 O ATOM 2889 N ALA 363 43.004 63.478 −63.137 1.00 36.83 N ATOM 2890 CA ALA 363 42.144 63.370 −64.312 1.00 36.83 C ATOM 2891 CB ALA 363 42.750 64.130 −65.475 1.00 36.83 C ATOM 2892 C ALA 363 42.003 61.889 −64.672 1.00 36.83 C ATOM 2893 O ALA 363 40.909 61.316 −64.569 1.00 36.83 O ATOM 2894 N GLY 364 43.111 61.272 −65.091 1.00 36.83 N ATOM 2895 CA GLY 364 43.083 59.864 −65.446 1.00 36.83 C ATOM 2896 C GLY 364 43.278 59.000 −64.219 1.00 36.83 C ATOM 2897 O GLY 364 42.748 59.313 −63.151 1.00 36.83 O ATOM 2898 N GLU 365 44.020 57.903 −64.365 1.00 36.83 N ATOM 2899 CA GLU 365 44.299 57.022 −63.226 1.00 36.83 C ATOM 2900 CB GLU 365 44.480 55.563 −63.667 1.00 36.83 C ATOM 2901 CG GLU 365 45.060 54.686 −62.527 1.00 36.83 C ATOM 2902 CD GLU 365 44.534 53.256 −62.508 1.00 36.83 C ATOM 2903 OE1 GLU 365 44.704 52.531 −63.516 1.00 36.83 O ATOM 2904 OE2 GLU 365 43.958 52.855 −61.468 1.00 36.83 O ATOM 2905 C GLU 365 45.572 57.486 −62.525 1.00 36.83 C ATOM 2906 O GLU 365 45.810 57.152 −61.363 1.00 36.83 O ATOM 2907 N GLY 366 46.391 58.256 −63.239 1.00 36.83 N ATOM 2908 CA GLY 366 47.628 58.747 −62.665 1.00 36.83 C ATOM 2909 C GLY 366 47.343 59.584 −61.438 1.00 36.83 C ATOM 2910 O GLY 366 46.375 60.336 −61.414 1.00 36.83 O ATOM 2911 N ALA 367 48.192 59.447 −60.425 1.00 36.83 N ATOM 2912 CA ALA 367 48.064 60.172 −59.168 1.00 36.83 C ATOM 2913 CB ALA 367 48.785 59.408 −58.074 1.00 36.83 C ATOM 2914 C ALA 367 48.611 61.592 −59.243 1.00 36.83 C ATOM 2915 O ALA 367 49.484 61.878 −60.059 1.00 36.83 O ATOM 2916 N VAL 368 48.082 62.482 −58.396 1.00 36.83 N ATOM 2917 CA VAL 368 48.542 63.874 −58.342 1.00 36.83 C ATOM 2918 CB VAL 368 47.501 64.856 −58.980 1.00 36.83 C ATOM 2919 CG1 VAL 368 46.969 64.267 −60.286 1.00 36.83 C ATOM 2920 CG2 VAL 368 46.356 65.163 −58.009 1.00 36.83 C ATOM 2921 C VAL 368 48.820 64.270 −56.883 1.00 36.83 C ATOM 2922 O VAL 368 48.533 63.502 −55.968 1.00 36.83 O ATOM 2923 N LEU 369 49.381 65.455 −56.667 1.00 36.83 N ATOM 2924 CA LEU 369 49.697 65.920 −55.318 1.00 36.83 C ATOM 2925 CB LEU 369 51.217 65.824 −55.110 1.00 36.83 C ATOM 2926 CG LEU 369 51.805 65.909 −53.693 1.00 36.83 C ATOM 2927 CD1 LEU 369 51.132 64.884 −52.760 1.00 36.83 C ATOM 2928 CD2 LEU 369 53.307 65.668 −53.763 1.00 36.83 C ATOM 2929 C LEU 369 49.201 67.368 −55.117 1.00 36.83 C ATOM 2930 O LEU 369 49.950 68.326 −55.272 1.00 36.83 O ATOM 2931 N LYS 370 47.931 67.527 −54.761 1.00 36.83 N ATOM 2932 CA LYS 370 47.354 68.864 −54.590 1.00 36.83 C ATOM 2933 CB LYS 370 45.890 68.751 −54.159 1.00 36.83 C ATOM 2934 CG LYS 370 44.999 68.245 −55.313 1.00 36.83 C ATOM 2935 CD LYS 370 43.574 67.929 −54.861 1.00 36.83 C ATOM 2936 CE LYS 370 42.762 67.261 −55.976 1.00 36.83 C ATOM 2937 NZ LYS 370 42.262 68.234 −57.010 1.00 36.83 N ATOM 2938 C LYS 370 48.144 69.756 −53.654 1.00 36.83 C ATOM 2939 O LYS 370 48.519 70.861 −54.027 1.00 36.83 O ATOM 2940 N ASP 371 48.401 69.295 −52.439 1.00 36.83 N ATOM 2941 CA ASP 371 49.196 70.092 −51.519 1.00 36.83 C ATOM 2942 CB ASP 371 48.587 70.061 −50.121 1.00 36.83 C ATOM 2943 CG ASP 371 49.536 70.581 −49.079 1.00 36.83 C ATOM 2944 OD1 ASP 371 50.270 69.756 −48.497 1.00 36.83 O ATOM 2945 OD2 ASP 371 49.567 71.815 −48.857 1.00 36.83 O ATOM 2946 C ASP 371 50.643 69.578 −51.495 1.00 36.83 C ATOM 2947 O ASP 371 50.883 68.381 −51.491 1.00 36.83 O ATOM 2948 N LYS 372 51.606 70.489 −51.494 1.00 36.83 N ATOM 2949 CA LYS 372 53.020 70.101 −51.501 1.00 36.83 C ATOM 2950 CB LYS 372 53.795 70.935 −52.538 1.00 36.83 C ATOM 2951 CG LYS 372 53.050 71.229 −53.829 1.00 36.83 C ATOM 2952 CD LYS 372 52.695 69.963 −54.578 1.00 36.83 C ATOM 2953 CE LYS 372 52.351 70.268 −56.025 1.00 36.83 C ATOM 2954 NZ LYS 372 52.033 69.040 −56.799 1.00 36.83 N ATOM 2955 C LYS 372 53.658 70.322 −50.136 1.00 36.83 C ATOM 2956 O LYS 372 54.861 70.158 −49.960 1.00 36.83 O ATOM 2957 N THR 373 52.847 70.688 −49.163 1.00 36.83 N ATOM 2958 CA THR 373 53.373 70.978 −47.850 1.00 36.83 C ATOM 2959 CB THR 373 52.229 71.265 −46.871 1.00 36.83 C ATOM 2960 OG1 THR 373 51.372 72.267 −47.438 1.00 36.83 O ATOM 2961 CG2 THR 373 52.775 71.778 −45.558 1.00 36.83 C ATOM 2962 C THR 373 54.299 69.909 −47.285 1.00 36.83 C ATOM 2963 O THR 373 55.383 70.228 −46.801 1.00 36.83 O ATOM 2964 N ALA 374 53.882 68.648 −47.343 1.00 36.83 N ATOM 2965 CA ALA 374 54.708 67.549 −46.828 1.00 36.83 C ATOM 2966 CB ALA 374 53.889 66.276 −46.731 1.00 36.83 C ATOM 2967 C ALA 374 55.906 67.329 −47.737 1.00 36.83 C ATOM 2968 O ALA 374 57.032 67.197 −47.266 1.00 36.83 O ATOM 2969 N LEU 375 55.660 67.315 −49.044 1.00 36.83 N ATOM 2970 CA LEU 375 56.726 67.110 −50.024 1.00 36.83 C ATOM 2971 CB LEU 375 56.162 67.205 −51.443 1.00 36.83 C ATOM 2972 CG LEU 375 57.179 67.129 −52.591 1.00 36.83 C ATOM 2973 CD1 LEU 375 57.748 65.729 −52.690 1.00 36.83 C ATOM 2974 CD2 LEU 375 56.502 67.518 −53.899 1.00 36.83 C ATOM 2975 C LEU 375 57.849 68.131 −49.838 1.00 36.83 C ATOM 2976 O LEU 375 59.026 67.771 −49.765 1.00 36.83 O ATOM 2977 N ASN 376 57.487 69.408 −49.753 1.00 36.83 N ATOM 2978 CA ASN 376 58.497 70.453 −49.573 1.00 36.83 C ATOM 2979 CB ASN 376 57.870 71.845 −49.673 1.00 36.83 C ATOM 2980 CG ASN 376 57.061 72.028 −50.925 1.00 36.83 C ATOM 2981 OD1 ASN 376 57.432 71.553 −52.000 1.00 36.83 O ATOM 2982 ND2 ASN 376 55.949 72.732 −50.801 1.00 36.83 N ATOM 2983 C ASN 376 59.202 70.320 −48.233 1.00 36.83 C ATOM 2984 O ASN 376 60.405 70.558 −48.134 1.00 36.83 O ATOM 2985 N ALA 377 58.451 69.948 −47.197 1.00 36.83 N ATOM 2986 CA ALA 377 59.043 69.776 −45.873 1.00 36.83 C ATOM 2987 CB ALA 377 57.987 69.281 −44.897 1.00 36.83 C ATOM 2988 C ALA 377 60.193 68.767 −45.963 1.00 36.83 C ATOM 2989 O ALA 377 61.364 69.087 −45.679 1.00 36.83 O ATOM 2990 N ALA 378 59.858 67.553 −46.374 1.00 36.83 N ATOM 2991 CA ALA 378 60.856 66.491 −46.503 1.00 36.83 C ATOM 2992 CB ALA 378 60.199 65.215 −46.989 1.00 36.83 C ATOM 2993 C ALA 378 61.980 66.875 −47.457 1.00 36.83 C ATOM 2994 O ALA 378 63.162 66.676 −47.158 1.00 36.83 O ATOM 2995 N SER 379 61.608 67.429 −48.604 1.00 36.83 N ATOM 2996 CA SER 379 62.590 67.820 −49.600 1.00 36.83 C ATOM 2997 CB SER 379 61.889 68.424 −50.815 1.00 36.83 C ATOM 2998 OG SER 379 60.994 67.474 −51.387 1.00 36.83 O ATOM 2999 C SER 379 63.546 68.807 −48.965 1.00 36.83 C ATOM 3000 O SER 379 64.759 68.724 −49.148 1.00 36.83 O ATOM 3001 N THR 380 62.992 69.721 −48.174 1.00 36.83 N ATOM 3002 CA THR 380 63.819 70.703 −47.495 1.00 36.83 C ATOM 3003 CB THR 380 62.978 71.663 −46.649 1.00 36.83 C ATOM 3004 OG1 THR 380 62.145 72.453 −47.510 1.00 36.83 O ATOM 3005 CG2 THR 380 63.892 72.576 −45.830 1.00 36.83 C ATOM 3006 C THR 380 64.863 70.044 −46.602 1.00 36.83 C ATOM 3007 O THR 380 66.055 70.202 −46.838 1.00 36.83 O ATOM 3008 N VAL 381 64.429 69.284 −45.596 1.00 36.83 N ATOM 3009 CA VAL 381 65.385 68.646 −44.681 1.00 36.83 C ATOM 3010 CB VAL 381 64.673 68.006 −43.448 1.00 36.83 C ATOM 3011 CG1 VAL 381 63.853 69.073 −42.710 1.00 36.83 C ATOM 3012 CG2 VAL 381 63.789 66.820 −43.880 1.00 36.83 C ATOM 3013 C VAL 381 66.316 67.610 −45.311 1.00 36.83 C ATOM 3014 O VAL 381 67.423 67.383 −44.802 1.00 36.83 O ATOM 3015 N PHE 382 65.884 66.991 −46.411 1.00 36.83 N ATOM 3016 CA PHE 382 66.704 65.990 −47.108 1.00 36.83 C ATOM 3017 CB PHE 382 65.837 65.065 −47.970 1.00 36.83 C ATOM 3018 CG PHE 382 65.190 63.939 −47.210 1.00 36.83 C ATOM 3019 CD1 PHE 382 65.932 63.158 −46.326 1.00 36.83 C ATOM 3020 CD2 PHE 382 63.843 63.642 −47.399 1.00 36.83 C ATOM 3021 CE1 PHE 382 65.335 62.090 −45.632 1.00 36.83 C ATOM 3022 CE2 PHE 382 63.235 62.571 −46.711 1.00 36.83 C ATOM 3023 CZ PHE 382 63.982 61.801 −45.831 1.00 36.83 C ATOM 3024 C PHE 382 67.773 66.601 −48.013 1.00 36.83 C ATOM 3025 O PHE 382 68.793 65.971 −48.297 1.00 36.83 O ATOM 3026 N GLY 383 67.545 67.820 −48.487 1.00 36.83 N ATOM 3027 CA GLY 383 68.534 68.438 −49.354 1.00 36.83 C ATOM 3028 C GLY 383 68.410 67.971 −50.791 1.00 36.83 C ATOM 3029 O GLY 383 69.418 67.708 −51.462 1.00 36.83 O ATOM 3030 N VAL 384 67.173 67.868 −51.266 1.00 36.83 N ATOM 3031 CA VAL 384 66.913 67.417 −52.626 1.00 36.83 C ATOM 3032 CB VAL 384 66.472 65.918 −52.649 1.00 36.83 C ATOM 3033 CG1 VAL 384 67.524 65.056 −51.970 1.00 36.83 C ATOM 3034 CG2 VAL 384 65.154 65.739 −51.947 1.00 36.83 C ATOM 3035 C VAL 384 65.824 68.277 −53.253 1.00 36.83 C ATOM 3036 O VAL 384 65.029 68.894 −52.546 1.00 36.83 O ATOM 3037 N ASN 385 65.798 68.312 −54.581 1.00 36.83 N ATOM 3038 CA ASN 385 64.820 69.105 −55.330 1.00 36.83 C ATOM 3039 CB ASN 385 65.279 69.239 −56.789 1.00 36.83 C ATOM 3040 CG ASN 385 64.340 70.084 −57.606 1.00 36.83 C ATOM 3041 OD1 ASN 385 63.141 69.798 −57.682 1.00 36.83 O ATOM 3042 ND2 ASN 385 64.866 71.140 −58.216 1.00 36.83 N ATOM 3043 C ASN 385 63.412 68.506 −55.286 1.00 36.83 C ATOM 3044 O ASN 385 63.166 67.420 −55.807 1.00 36.83 O ATOM 3045 N PRO 386 62.459 69.219 −54.676 1.00 36.83 N ATOM 3046 CD PRO 386 62.546 70.587 −54.137 1.00 36.83 C ATOM 3047 CA PRO 386 61.086 68.715 −54.584 1.00 36.83 C ATOM 3048 CB PRO 386 60.355 69.850 −53.861 1.00 36.83 C ATOM 3049 CG PRO 386 61.120 71.062 −54.284 1.00 36.83 C ATOM 3050 C PRO 386 60.394 68.308 −55.894 1.00 36.83 C ATOM 3051 O PRO 386 59.664 67.313 −55.930 1.00 36.83 O ATOM 3052 N SER 387 60.582 69.076 −56.961 1.00 36.83 N ATOM 3053 CA SER 387 59.935 68.724 −58.214 1.00 36.83 C ATOM 3054 CB SER 387 59.998 69.886 −59.205 1.00 36.83 C ATOM 3055 OG SER 387 59.084 70.900 −58.831 1.00 36.83 O ATOM 3056 C SER 387 60.555 67.475 −58.814 1.00 36.83 C ATOM 3057 O SER 387 59.872 66.724 −59.511 1.00 36.83 O ATOM 3058 N VAL 388 61.842 67.247 −58.539 1.00 36.83 N ATOM 3059 CA VAL 388 62.505 66.047 −59.037 1.00 36.83 C ATOM 3060 CB VAL 388 64.045 66.068 −58.820 1.00 36.83 C ATOM 3061 CG1 VAL 388 64.613 64.671 −59.032 1.00 36.83 C ATOM 3062 CG2 VAL 388 64.716 67.022 −59.793 1.00 36.83 C ATOM 3063 C VAL 388 61.933 64.866 −58.256 1.00 36.83 C ATOM 3064 O VAL 388 61.626 63.828 −58.829 1.00 36.83 O ATOM 3065 N LEU 389 61.790 65.047 −56.944 1.00 36.83 N ATOM 3066 CA LEU 389 61.262 64.005 −56.060 1.00 36.83 C ATOM 3067 CB LEU 389 61.325 64.468 −54.601 1.00 36.83 C ATOM 3068 CG LEU 389 60.677 63.562 −53.541 1.00 36.83 C ATOM 3069 CD1 LEU 389 61.353 62.193 −53.501 1.00 36.83 C ATOM 3070 CD2 LEU 389 60.776 64.243 −52.189 1.00 36.83 C ATOM 3071 C LEU 389 59.825 63.646 −56.408 1.00 36.83 C ATOM 3072 O LEU 389 59.465 62.466 −56.520 1.00 36.83 O ATOM 3073 N GLU 390 59.008 64.681 −56.568 1.00 36.83 N ATOM 3074 CA GLU 390 57.611 64.504 −56.901 1.00 36.83 C ATOM 3075 CB GLU 390 56.959 65.861 −57.141 1.00 36.83 C ATOM 3076 CG GLU 390 55.533 65.739 −57.567 1.00 36.83 C ATOM 3077 CD GLU 390 54.920 67.054 −57.981 1.00 36.83 C ATOM 3078 OE1 GLU 390 53.732 67.028 −58.366 1.00 36.83 O ATOM 3079 OE2 GLU 390 55.615 68.101 −57.925 1.00 36.83 O ATOM 3080 C GLU 390 57.506 63.652 −58.151 1.00 36.83 C ATOM 3081 O GLU 390 56.799 62.633 −58.172 1.00 36.83 O ATOM 3082 N LYS 391 58.237 64.065 −59.182 1.00 36.83 N ATOM 3083 CA LYS 391 58.266 63.370 −60.463 1.00 36.83 C ATOM 3084 CB LYS 391 59.271 64.050 −61.395 1.00 36.83 C ATOM 3085 CG LYS 391 58.837 64.083 −62.837 1.00 36.83 C ATOM 3086 CD LYS 391 57.756 65.114 −63.066 1.00 36.83 C ATOM 3087 CE LYS 391 58.321 66.533 −62.959 1.00 36.83 C ATOM 3088 NZ LYS 391 59.235 66.901 −64.088 1.00 36.83 N ATOM 3089 C LYS 391 58.654 61.904 −60.302 1.00 36.83 C ATOM 3090 O LYS 391 58.010 61.019 −60.846 1.00 36.83 O ATOM 3091 N ALA 392 59.714 61.660 −59.545 1.00 36.83 N ATOM 3092 CA ALA 392 60.212 60.305 −59.326 1.00 36.83 C ATOM 3093 CB ALA 392 61.542 60.362 −58.585 1.00 36.83 C ATOM 3094 C ALA 392 59.230 59.434 −58.552 1.00 36.83 C ATOM 3095 O ALA 392 59.227 58.210 −58.692 1.00 36.83 O ATOM 3096 N LEU 393 58.395 60.079 −57.749 1.00 36.83 N ATOM 3097 CA LEU 393 57.413 59.398 −56.921 1.00 36.83 C ATOM 3098 CB LEU 393 56.982 60.324 −55.781 1.00 36.83 C ATOM 3099 CG LEU 393 57.024 59.882 −54.320 1.00 36.83 C ATOM 3100 CD1 LEU 393 58.416 59.464 −53.903 1.00 36.83 C ATOM 3101 CD2 LEU 393 56.531 61.054 −53.461 1.00 36.83 C ATOM 3102 C LEU 393 56.179 58.944 −57.687 1.00 36.83 C ATOM 3103 O LEU 393 55.692 57.836 −57.480 1.00 36.83 O ATOM 3104 N MET 394 55.681 59.789 −58.581 1.00 36.83 N ATOM 3105 CA MET 394 54.475 59.467 −59.332 1.00 36.83 C ATOM 3106 CB MET 394 53.498 60.632 −59.217 1.00 36.83 C ATOM 3107 CG MET 394 53.432 61.198 −57.819 1.00 36.83 C ATOM 3108 SD MET 394 52.154 62.442 −57.628 1.00 36.83 S ATOM 3109 CE MET 394 53.128 63.950 −57.823 1.00 36.83 C ATOM 3110 C MET 394 54.722 59.150 −60.801 1.00 36.83 C ATOM 3111 O MET 394 53.890 58.518 −61.461 1.00 36.83 O ATOM 3112 N GLU 395 55.871 59.589 −61.307 1.00 36.83 N ATOM 3113 CA GLU 395 56.209 59.367 −62.706 1.00 36.83 C ATOM 3114 CB GLU 395 55.972 60.650 −63.509 1.00 36.83 C ATOM 3115 CG GLU 395 54.537 61.160 −63.434 1.00 36.83 C ATOM 3116 CD GLU 395 54.296 62.406 −64.293 1.00 36.83 C ATOM 3117 OE1 GLU 395 54.353 62.309 −65.540 1.00 36.83 O ATOM 3118 OE2 GLU 395 54.054 63.487 −63.716 1.00 36.83 O ATOM 3119 C GLU 395 57.649 58.885 −62.903 1.00 36.83 C ATOM 3120 O GLU 395 58.441 59.519 −63.598 1.00 36.83 O ATOM 3121 N PRO 396 58.004 57.746 −62.293 1.00 36.83 N ATOM 3122 CD PRO 396 57.191 56.860 −61.439 1.00 36.83 C ATOM 3123 CA PRO 396 59.364 57.225 −62.446 1.00 36.83 C ATOM 3124 CB PRO 396 59.414 56.108 −61.403 1.00 36.83 C ATOM 3125 CG PRO 396 58.010 55.578 −61.427 1.00 36.83 C ATOM 3126 C PRO 396 59.571 56.702 −63.872 1.00 36.83 C ATOM 3127 O PRO 396 58.625 56.239 −64.508 1.00 36.83 O ATOM 3128 N ARG 397 60.805 56.773 −64.368 1.00 36.83 N ATOM 3129 CA ARG 397 61.116 56.295 −65.714 1.00 36.83 C ATOM 3130 CB ARG 397 62.110 57.236 −66.401 1.00 36.83 C ATOM 3131 CG ARG 397 61.710 58.696 −66.401 1.00 36.83 C ATOM 3132 CD ARG 397 62.750 59.493 −65.660 1.00 36.83 C ATOM 3133 NE ARG 397 63.806 60.009 −66.518 1.00 36.83 N ATOM 3134 CZ ARG 397 65.027 60.319 −66.085 1.00 36.83 C ATOM 3135 NH1 ARG 397 65.338 60.143 −64.809 1.00 36.83 N ATOM 3136 NH2 ARG 397 65.926 60.833 −66.921 1.00 36.83 N ATOM 3137 C ARG 397 61.736 54.912 −65.670 1.00 36.83 C ATOM 3138 O ARG 397 62.633 54.670 −64.880 1.00 36.83 O ATOM 3139 N ILE 398 61.262 53.999 −66.504 1.00 36.83 N ATOM 3140 CA ILE 398 61.848 52.659 −66.551 1.00 36.83 C ATOM 3141 CB ILE 398 60.895 51.560 −66.010 1.00 36.83 C ATOM 3142 CG2 ILE 398 60.641 51.761 −64.512 1.00 36.83 C ATOM 3143 CG1 ILE 398 59.591 51.563 −66.813 1.00 36.83 C ATOM 3144 CD1 ILE 398 58.662 50.435 −66.458 1.00 36.83 C ATOM 3145 C ILE 398 62.116 52.349 −68.012 1.00 36.83 C ATOM 3146 O ILE 398 61.797 53.153 −68.892 1.00 36.83 O ATOM 3147 N LEU 399 62.699 51.185 −68.269 1.00 36.83 N ATOM 3148 CA LEU 399 62.962 50.759 −69.633 1.00 36.83 C ATOM 3149 CB LEU 399 64.333 50.099 −69.745 1.00 36.83 C ATOM 3150 CG LEU 399 65.537 50.827 −69.175 1.00 36.83 C ATOM 3151 CD1 LEU 399 65.590 50.540 −67.678 1.00 36.83 C ATOM 3152 CD2 LEU 399 66.816 50.358 −69.868 1.00 36.83 C ATOM 3153 C LEU 399 61.915 49.746 −70.071 1.00 36.83 C ATOM 3154 O LEU 399 61.446 48.940 −69.277 1.00 36.83 O ATOM 3155 N ALA 400 61.539 49.818 −71.335 1.00 36.83 N ATOM 3156 CA ALA 400 60.589 48.893 −71.942 1.00 36.83 C ATOM 3157 CB ALA 400 59.355 49.627 −72.418 1.00 36.83 C ATOM 3158 C ALA 400 61.416 48.396 −73.125 1.00 36.83 C ATOM 3159 O ALA 400 61.354 48.952 −74.221 1.00 36.83 O ATOM 3160 N GLY 401 62.214 47.361 −72.866 1.00 36.83 N ATOM 3161 CA GLY 401 63.116 96.832 −73.875 1.00 36.83 C ATOM 3162 C GLY 401 64.323 47.738 −73.716 1.00 36.83 C ATOM 3163 O GLY 401 65.069 47.605 −72.746 1.00 36.83 O ATOM 3164 N ARG 402 64.506 48.674 −74.641 1.00 36.83 N ATOM 3165 CA ARG 402 65.609 49.631 −74.536 1.00 36.83 C ATOM 3166 CB ARG 402 66.604 49.429 −75.684 1.00 36.83 C ATOM 3167 CG ARG 402 67.514 48.225 −75.465 1.00 36.83 C ATOM 3168 CD ARG 402 68.423 47.976 −76.648 1.00 36.83 C ATOM 3169 NE ARG 402 69.352 46.891 −76.363 1.00 36.83 N ATOM 3170 CZ ARG 402 70.567 47.056 −75.859 1.00 36.83 C ATOM 3171 NH1 ARG 402 71.017 48.279 −75.588 1.00 36.83 N ATOM 3172 NH2 ARG 402 71.322 45.985 −75.615 1.00 36.83 N ATOM 3173 C ARG 402 65.087 51.073 −74.519 1.00 36.83 C ATOM 3174 O ARG 402 65.824 52.008 −74.229 1.00 36.83 O ATOM 3175 N ASP 403 63.800 51.229 −74.810 1.00 36.83 N ATOM 3176 CA ASP 403 63.149 52.534 −74.841 1.00 36.83 C ATOM 3177 CB ASP 403 61.789 52.400 −75.532 1.00 36.83 C ATOM 3178 CG ASP 403 61.188 53.735 −75.911 1.00 36.83 C ATOM 3179 OD1 ASP 403 61.734 54.791 −75.533 1.00 36.83 O ATOM 3180 OD2 ASP 403 60.157 53.729 −76.599 1.00 36.83 O ATOM 3181 C ASP 403 62.964 53.095 −73.426 1.00 36.83 C ATOM 3182 O ASP 403 62.702 52.341 −72.476 1.00 36.83 O ATOM 3183 N LEU 404 63.119 54.407 −73.272 1.00 36.83 N ATOM 3184 CA LEU 404 62.962 55.036 −71.964 1.00 36.83 C ATOM 3185 CB LEU 404 63.892 56.238 −71.815 1.00 36.83 C ATOM 3186 CG LEU 404 63.985 56.818 −70.396 1.00 36.83 C ATOM 3187 CD1 LEU 404 64.460 55.752 −69.415 1.00 36.83 C ATOM 3188 CD2 LEU 404 64.952 57.979 −70.393 1.00 36.83 C ATOM 3189 C LEU 404 61.528 55.492 −71.856 1.00 36.83 C ATOM 3190 O LEU 404 61.119 56.465 −72.509 1.00 36.83 O ATOM 3191 N VAL 405 60.761 54.798 −71.024 1.00 36.83 N ATOM 3192 CA VAL 405 59.344 55.096 −70.858 1.00 36.83 C ATOM 3193 CB VAL 405 58.506 53.846 −71.212 1.00 36.83 C ATOM 3194 CG1 VAL 405 57.064 54.058 −70.857 1.00 36.83 C ATOM 3195 CG2 VAL 405 58.634 53.556 −72.689 1.00 36.83 C ATOM 3196 C VAL 405 58.971 55.575 −69.457 1.00 36.83 C ATOM 3197 O VAL 405 59.156 54.870 −68.474 1.00 36.83 O ATOM 3198 N ALA 406 58.436 56.781 −69.368 1.00 36.83 N ATOM 3199 CA ALA 406 58.047 57.311 −68.072 1.00 36.83 C ATOM 3200 CB ALA 406 58.136 58.838 −68.054 1.00 36.83 C ATOM 3201 C ALA 406 56.626 56.883 −67.840 1.00 36.83 C ATOM 3202 O ALA 406 55.782 57.016 −68.714 1.00 36.83 O ATOM 3203 N GLN 407 56.354 56.345 −66.664 1.00 36.83 N ATOM 3204 CA GLN 407 55.000 55.940 −66.365 1.00 36.83 C ATOM 3205 CB GLN 407 54.972 54.537 −65.770 1.00 36.83 C ATOM 3206 CG GLN 407 56.173 54.184 −64.923 1.00 36.83 C ATOM 3207 CD GLN 407 56.096 52.746 −64.470 1.00 36.83 C ATOM 3208 OE1 GLN 407 55.679 51.874 −65.235 1.00 36.83 O ATOM 3209 NE2 GLN 407 56.492 52.486 −63.229 1.00 36.83 N ATOM 3210 C GLN 407 54.388 56.922 −65.394 1.00 36.83 C ATOM 3211 O GLN 407 55.042 57.853 −64.927 1.00 36.83 O ATOM 3212 N HIS 408 53.111 56.713 −65.117 1.00 36.83 N ATOM 3213 CA HIS 408 52.391 57.549 −64.189 1.00 36.83 C ATOM 3214 CB HIS 408 51.419 58.468 −64.943 1.00 36.83 C ATOM 3215 CG HIS 408 50.830 59.549 −64.090 1.00 36.83 C ATOM 3216 CD2 HIS 408 50.954 59.805 −62.767 1.00 36.83 C ATOM 3217 ND1 HIS 408 49.998 60.529 −64.596 1.00 36.83 N ATOM 3218 CE1 HIS 408 49.638 61.341 −63.618 1.00 36.83 C ATOM 3219 NE2 HIS 408 50.203 60.924 −62.498 1.00 36.83 N ATOM 3220 C HIS 408 51.649 56.553 −63.319 1.00 36.83 C ATOM 3221 O HIS 408 50.707 55.892 −63.770 1.00 36.83 O ATOM 3222 N LEU 409 52.106 56.432 −62.077 1.00 36.83 N ATOM 3223 CA LEU 409 51.519 55.506 −61.118 1.00 36.83 C ATOM 3224 CB LEU 409 52.510 55.246 −59.979 1.00 36.83 C ATOM 3225 CG LEU 409 53.916 54.769 −60.340 1.00 36.83 C ATOM 3226 CD1 LEU 409 54.733 54.700 −59.075 1.00 36.83 C ATOM 3227 CD2 LEU 409 53.867 53.411 −61.041 1.00 36.83 C ATOM 3228 C LEU 409 50.226 56.059 −60.529 1.00 36.83 C ATOM 3229 O LEU 409 50.031 57.279 −60.479 1.00 36.83 O ATOM 3230 N ASN 410 49.337 55.171 −60.094 1.00 36.83 N ATOM 3231 CA ASN 410 48.095 55.633 −59.470 1.00 36.83 C ATOM 3232 CB ASN 410 47.014 54.554 −59.497 1.00 36.83 C ATOM 3233 CG ASN 410 47.495 53.247 −58.948 1.00 36.83 C ATOM 3234 OD1 ASN 410 48.430 53.209 −58.152 1.00 36.83 O ATOM 3235 ND2 ASN 410 46.856 52.161 −59.356 1.00 36.83 N ATOM 3236 C ASN 410 48.402 56.005 −58.020 1.00 36.83 C ATOM 3237 O ASN 410 49.556 56.221 −57.654 1.00 36.83 O ATOM 3238 N VAL 411 47.369 56.063 −57.195 1.00 36.83 N ATOM 3239 CA VAL 411 47.533 56.423 −55.797 1.00 36.83 C ATOM 3240 CB VAL 411 46.168 56.761 −55.174 1.00 36.83 C ATOM 3241 CG1 VAL 411 46.338 57.254 −53.748 1.00 36.83 C ATOM 3242 CG2 VAL 411 45.476 57.810 −56.019 1.00 36.83 C ATOM 3243 C VAL 411 48.174 55.283 −55.029 1.00 36.83 C ATOM 3244 O VAL 411 49.133 55.473 −54.296 1.00 36.83 O ATOM 3245 N GLU 412 47.648 54.085 −55.214 1.00 36.83 N ATOM 3246 CA GLU 412 48.178 52.933 −54.509 1.00 36.83 C ATOM 3247 CB GLU 412 47.327 51.692 −54.820 1.00 36.83 C ATOM 3248 CG GLU 412 47.516 50.583 −53.793 1.00 36.83 C ATOM 3249 CD GLU 412 46.401 49.534 −53.818 1.00 36.83 C ATOM 3250 OE1 GLU 412 46.476 48.576 −52.999 1.00 36.83 O ATOM 3251 OE2 GLU 412 45.458 49.678 −54.644 1.00 36.83 O ATOM 3252 C GLU 412 49.658 52.674 −54.838 1.00 36.83 C ATOM 3253 O GLU 412 50.437 52.330 −53.952 1.00 36.83 O ATOM 3254 N LYS 413 50.038 52.869 −56.098 1.00 36.83 N ATOM 3255 CA LYS 413 51.410 52.642 −56.530 1.00 36.83 C ATOM 3256 CB LYS 413 51.487 52.612 −58.053 1.00 36.83 C ATOM 3257 CG LYS 413 51.809 51.257 −58.660 1.00 36.83 C ATOM 3258 CD LYS 413 50.632 50.291 −58.614 1.00 36.83 C ATOM 3259 CE LYS 413 50.898 49.100 −59.537 1.00 36.83 C ATOM 3260 NZ LYS 413 50.027 47.925 −59.264 1.00 36.83 N ATOM 3261 C LYS 413 52.369 53.699 −56.008 1.00 36.83 C ATOM 3262 O LYS 413 53.479 53.377 −55.598 1.00 36.83 O ATOM 3263 N SER 414 51.948 54.962 −56.043 1.00 36.83 N ATOM 3264 CA SER 414 52.784 56.063 −55.556 1.00 36.83 C ATOM 3265 CB SER 414 52.135 57.419 −55.845 1.00 36.83 C ATOM 3266 OG SER 414 51.719 57.505 −57.189 1.00 36.83 O ATOM 3267 C SER 414 52.993 55.935 −54.056 1.00 36.83 C ATOM 3268 O SER 414 54.087 56.139 −53.559 1.00 36.83 O ATOM 3269 N SER 415 51.933 55.598 −53.334 1.00 36.83 N ATOM 3270 CA SER 415 52.027 55.444 −51.887 1.00 36.83 C ATOM 3271 CB SER 415 50.662 55.059 −51.313 1.00 36.83 C ATOM 3272 OG SER 415 50.643 55.206 −49.900 1.00 36.83 O ATOM 3273 C SER 415 53.078 54.365 −51.564 1.00 36.83 C ATOM 3274 O SER 415 53.933 54.559 −50.698 1.00 36.83 O ATOM 3275 N SER 416 53.007 53.244 −52.279 1.00 36.83 N ATOM 3276 CA SER 416 53.942 52.140 −52.113 1.00 36.83 C ATOM 3277 CB SER 416 53.536 50.967 −52.994 1.00 36.83 C ATOM 3278 OG SER 416 52.367 50.364 −52.472 1.00 36.83 O ATOM 3279 C SER 416 55.386 52.523 −52.418 1.00 36.83 C ATOM 3280 O SER 416 56.283 52.152 −51.667 1.00 36.83 O ATOM 3281 N SER 417 55.605 53.257 −53.513 1.00 36.83 N ATOM 3282 CA SER 417 56.950 53.699 −53.887 1.00 36.83 C ATOM 3283 CB SER 417 56.921 54.506 −55.202 1.00 36.83 C ATOM 3284 OG SER 417 58.208 55.018 −55.547 1.00 36.83 O ATOM 3285 C SER 417 57.477 54.566 −52.753 1.00 36.83 C ATOM 3286 O SER 417 58.591 54.368 −52.282 1.00 36.83 O ATOM 3287 N ARG 418 56.659 55.516 −52.311 1.00 36.83 N ATOM 3288 CA ARG 418 57.013 56.406 −51.203 1.00 36.83 C ATOM 3289 CB ARG 418 55.811 57.311 −50.855 1.00 36.83 C ATOM 3290 CG ARG 418 55.973 58.220 −49.626 1.00 36.83 C ATOM 3291 CD ARG 418 55.455 57.556 −48.346 1.00 36.83 C ATOM 3292 NE ARG 418 54.036 57.203 −48.440 1.00 36.83 N ATOM 3293 CZ ARG 418 53.036 58.085 −48.412 1.00 36.83 C ATOM 3294 NH1 ARG 418 53.283 59.381 −48.283 1.00 36.83 N ATOM 3295 NH2 ARG 418 51.788 57.679 −48.534 1.00 36.83 N ATOM 3296 C ARG 418 57.436 55.565 −49.992 1.00 36.83 C ATOM 3297 O ARG 418 58.463 55.836 −49.369 1.00 36.83 O ATOM 3298 N ASP 419 56.652 54.536 −49.667 1.00 36.83 N ATOM 3299 CA ASP 419 56.996 53.675 −48.536 1.00 36.83 C ATOM 3300 CB ASP 419 55.922 52.607 −48.306 1.00 36.83 C ATOM 3301 CG ASP 419 54.673 53.161 −47.655 1.00 36.83 C ATOM 3302 OD1 ASP 419 54.669 54.340 −47.223 1.00 36.83 O ATOM 3303 OD2 ASP 419 53.687 52.400 −47.566 1.00 36.83 O ATOM 3304 C ASP 419 58.348 53.000 −48.762 1.00 36.83 C ATOM 3305 O ASP 419 59.152 52.875 −47.827 1.00 36.83 O ATOM 3306 N ALA 420 58.585 52.571 −50.004 1.00 36.83 N ATOM 3307 CA ALA 420 59.844 51.922 −50.384 1.00 36.83 C ATOM 3308 CB ALA 420 59.803 51.498 −51.853 1.00 36.83 C ATOM 3309 C ALA 420 61.015 52.876 −50.160 1.00 36.83 C ATOM 3310 O ALA 420 62.049 52.477 −49.645 1.00 36.83 O ATOM 3311 N LEU 421 60.851 54.130 −50.575 1.00 36.83 N ATOM 3312 CA LEU 421 61.896 55.131 −50.391 1.00 36.83 C ATOM 3313 CB LEU 421 61.488 56.481 −50.999 1.00 36.83 C ATOM 3314 CG LEU 421 62.376 57.671 −50.593 1.00 36.83 C ATOM 3315 CD1 LEU 421 63.816 57.400 −51.026 1.00 36.83 C ATOM 3316 CD2 LEU 421 61.853 58.983 −51.208 1.00 36.83 C ATOM 3317 C LEU 421 62.105 55.290 −48.895 1.00 36.83 C ATOM 3318 O LEU 421 63.235 55.361 −48.428 1.00 36.83 O ATOM 3319 N VAL 422 61.009 55.330 −48.143 1.00 36.83 N ATOM 3320 CA VAL 422 61.101 55.470 −46.690 1.00 36.83 C ATOM 3321 CB VAL 422 59.688 55.589 −46.032 1.00 36.83 C ATOM 3322 CG1 VAL 422 59.743 55.161 −44.566 1.00 36.83 C ATOM 3323 CG2 VAL 422 59.197 57.034 −46.136 1.00 36.83 C ATOM 3324 C VAL 422 61.874 54.319 −46.034 1.00 36.83 C ATOM 3325 O VAL 422 62.786 54.563 −45.242 1.00 36.83 O ATOM 3326 N LYS 423 61.504 53.079 −46.364 1.00 36.83 N ATOM 3327 CA LYS 423 62.167 51.902 −45.804 1.00 36.83 C ATOM 3328 CB LYS 423 61.417 50.630 −46.209 1.00 36.83 C ATOM 3329 CG LYS 423 60.147 50.422 −45.413 1.00 36.83 C ATOM 3330 CD LYS 423 59.037 49.852 −46.253 1.00 36.83 C ATOM 3331 CE LYS 423 59.098 48.349 −46.337 1.00 36.83 C ATOM 3332 NZ LYS 423 57.893 47.817 −47.047 1.00 36.83 N ATOM 3333 C LYS 423 63.630 51.801 −46.224 1.00 36.83 C ATOM 3334 O LYS 423 64.463 51.350 −45.457 1.00 36.83 O ATOM 3335 N ALA 424 63.932 52.214 −47.446 1.00 36.83 N ATOM 3336 CA ALA 424 65.297 52.181 −47.945 1.00 36.83 C ATOM 3337 CB ALA 424 65.321 52.492 −49.431 1.00 36.83 C ATOM 3338 C ALA 424 66.099 53.216 −47.169 1.00 36.83 C ATOM 3339 O ALA 424 67.258 52.987 −46.837 1.00 36.83 O ATOM 3340 N LEU 425 65.483 54.355 −46.877 1.00 36.83 N ATOM 3341 CA LEU 425 66.174 55.391 −46.107 1.00 36.83 C ATOM 3342 CB LEU 425 65.331 56.679 −46.025 1.00 36.83 C ATOM 3343 CG LEU 425 65.347 57.609 −47.245 1.00 36.83 C ATOM 3344 CD1 LEU 425 64.145 58.542 −47.196 1.00 36.83 C ATOM 3345 CD2 LEU 425 66.639 58.404 −47.282 1.00 36.83 C ATOM 3346 C LEU 425 66.515 54.920 −44.697 1.00 36.83 C ATOM 3347 O LEU 425 67.673 54.940 −44.303 1.00 36.83 O ATOM 3348 N TYR 426 65.511 54.480 −43.942 1.00 36.83 N ATOM 3349 CA TYR 426 65.747 54.046 −42.560 1.00 36.83 C ATOM 3350 CB TYR 426 64.429 53.636 −41.889 1.00 36.83 C ATOM 3351 CG TYR 426 64.493 53.628 −40.376 1.00 36.83 C ATOM 3352 CD1 TYR 426 64.323 54.806 −39.644 1.00 36.83 C ATOM 3353 CE1 TYR 426 64.408 54.819 −38.261 1.00 36.83 C ATOM 3354 CD2 TYR 426 64.749 52.449 −39.674 1.00 36.83 C ATOM 3355 CE2 TYR 426 64.836 52.449 −38.284 1.00 36.83 C ATOM 3356 CZ TYR 426 64.667 53.641 −37.584 1.00 36.83 C ATOM 3357 OH TYR 426 64.768 53.653 −36.217 1.00 36.83 O ATOM 3358 C TYR 426 66.744 52.889 −42.497 1.00 36.83 C ATOM 3359 O TYR 426 67.683 52.902 −41.684 1.00 36.83 O ATOM 3360 N GLY 427 66.541 51.904 −43.370 1.00 36.83 N ATOM 3361 CA GLY 427 67.419 50.747 −43.420 1.00 36.83 C ATOM 3362 C GLY 427 68.891 51.057 −43.688 1.00 36.83 C ATOM 3363 O GLY 427 69.784 50.461 −43.077 1.00 36.83 O ATOM 3364 N ARG 428 69.161 51.979 −44.603 1.00 36.83 N ATOM 3365 CA ARG 428 70.549 52.319 −44.895 1.00 36.83 C ATOM 3366 CB ARG 428 70.661 53.038 −46.231 1.00 36.83 C ATOM 3367 CG ARG 428 70.273 52.178 −47.395 1.00 36.83 C ATOM 3368 CD ARG 428 70.264 52.970 −48.681 1.00 36.83 C ATOM 3369 NE ARG 428 69.777 52.147 −49.780 1.00 36.83 N ATOM 3370 CZ ARG 428 69.742 52.519 −51.053 1.00 36.83 C ATOM 3371 NH1 ARG 428 70.172 53.717 −51.422 1.00 36.83 N ATOM 3372 NH2 ARG 428 69.260 51.684 −51.955 1.00 36.83 N ATOM 3373 C ARG 428 71.098 53.187 −43.784 1.00 36.83 C ATOM 3374 O ARG 428 72.295 53.214 −43.556 1.00 36.83 O ATOM 3375 N LEU 429 70.220 53.903 −43.089 1.00 36.83 N ATOM 3376 CA LEU 429 70.670 54.735 −41.985 1.00 36.83 C ATOM 3377 CB LEU 429 69.529 55.616 −41.443 1.00 36.83 C ATOM 3378 CG LEU 429 69.891 56.417 −40.178 1.00 36.83 C ATOM 3379 CD1 LEU 429 71.083 57.344 −40.451 1.00 36.83 C ATOM 3380 CD2 LEU 429 68.700 57.219 −39.695 1.00 36.83 C ATOM 3381 C LEU 429 71.181 53.805 −40.893 1.00 36.83 C ATOM 3382 O LEU 429 72.251 54.035 −40.316 1.00 36.83 O ATOM 3383 N PHE 430 70.434 52.733 −40.639 1.00 36.83 N ATOM 3384 CA PHE 430 70.802 51.771 −39.603 1.00 36.83 C ATOM 3385 CB PHE 430 69.700 50.720 −39.430 1.00 36.83 C ATOM 3386 CG PHE 430 69.777 49.961 −38.132 1.00 36.83 C ATOM 3387 CD1 PHE 430 69.227 50.490 −36.968 1.00 36.83 C ATOM 3388 CD2 PHE 430 70.414 48.726 −38.066 1.00 36.83 C ATOM 3389 CE1 PHE 430 69.314 49.805 −35.756 1.00 36.83 C ATOM 3390 CE2 PHE 430 70.505 48.032 −36.862 1.00 36.83 C ATOM 3391 CZ PHE 430 69.956 48.574 −35.706 1.00 36.83 C ATOM 3392 C PHE 430 72.118 51.079 −39.942 1.00 36.83 C ATOM 3393 O PHE 430 72.991 50.927 −39.092 1.00 36.83 O ATOM 3394 N LEU 431 72.270 50.613 −41.158 1.00 36.83 N ATOM 3395 CA LEU 431 73.510 50.003 −41.558 1.00 36.83 C ATOM 3396 CB LEU 431 73.390 49.502 −42.977 1.00 36.83 C ATOM 3397 CG LEU 431 73.169 48.035 −43.283 1.00 36.83 C ATOM 3398 CD1 LEU 431 72.355 47.301 −42.271 1.00 36.83 C ATOM 3399 CD2 LEU 431 72.588 47.891 −44.653 1.00 36.83 C ATOM 3400 C LEU 431 74.653 51.008 −41.463 1.00 36.83 C ATOM 3401 O LEU 431 75.728 50.684 −41.071 1.00 36.83 O ATOM 3402 N TRP 432 74.390 52.236 −41.843 1.00 36.83 N ATOM 3403 CA TRP 432 75.392 53.289 −41.728 1.00 36.83 C ATOM 3404 CB TRP 432 74.825 54.606 −42.273 1.00 36.83 C ATOM 3405 CG TRP 432 75.824 55.725 −42.364 1.00 36.83 C ATOM 3406 CD2 TRP 432 75.915 56.853 −41.497 1.00 36.83 C ATOM 3407 CE2 TRP 432 77.016 57.627 −41.927 1.00 36.83 C ATOM 3408 CE3 TRP 432 75.174 57.287 −40.395 1.00 36.83 C ATOM 3409 CD1 TRP 432 76.852 55.856 −43.272 1.00 36.83 C ATOM 3410 NE1 TRP 432 77.571 56.999 −43.012 1.00 36.83 N ATOM 3411 CZ2 TRP 432 77.388 58.804 −41.289 1.00 36.83 C ATOM 3412 CZ3 TRP 432 75.549 58.466 −39.761 1.00 36.83 C ATOM 3413 CH2 TRP 432 76.644 59.207 −40.211 1.00 36.83 C ATOM 3414 C TRP 432 75.789 53.453 −40.250 1.00 36.83 C ATOM 3415 O TRP 432 76.977 53.423 −39.914 1.00 36.83 O ATOM 3416 N LEU 433 74.799 53.619 −39.370 1.00 36.83 N ATOM 3417 CA LEU 433 75.075 53.765 −37.938 1.00 36.83 C ATOM 3418 CB LEU 433 73.776 53.838 −37.116 1.00 36.83 C ATOM 3419 CG LEU 433 72.812 55.027 −37.234 1.00 36.83 C ATOM 3420 CD1 LEU 433 71.608 54.773 −36.342 1.00 36.83 C ATOM 3421 CD2 LEU 433 73.499 56.334 −36.828 1.00 36.83 C ATOM 3422 C LEU 433 75.911 52.596 −37.421 1.00 36.83 C ATOM 3423 O LEU 433 76.755 52.766 −36.542 1.00 36.83 O ATOM 3424 N VAL 434 75.679 51.402 −37.956 1.00 36.83 N ATOM 3425 CA VAL 434 76.436 50.246 −37.498 1.00 36.83 C ATOM 3426 CB VAL 434 75.760 48.928 −37.900 1.00 36.83 C ATOM 3427 CG1 VAL 434 76.576 47.760 −37.380 1.00 36.83 C ATOM 3428 CG2 VAL 434 74.353 48.866 −37.316 1.00 36.83 C ATOM 3429 C VAL 434 77.889 50.234 −37.976 1.00 36.83 C ATOM 3430 O VAL 434 78.773 49.816 −37.234 1.00 36.83 O ATOM 3431 N ILE 435 78.155 50.677 −39.202 1.00 36.83 N ATOM 3432 CA ILE 435 79.540 50.690 −39.665 1.00 36.83 C ATOM 3433 CB ILE 435 79.672 50.854 −41.200 1.00 36.83 C ATOM 3434 CG2 ILE 435 78.933 49.718 −41.898 1.00 36.83 C ATOM 3435 CG1 ILE 435 79.160 52.222 −41.640 1.00 36.83 C ATOM 3436 CD1 ILE 435 79.402 52.515 −43.117 1.00 36.83 C ATOM 3437 C ILE 435 80.288 51.815 −38.973 1.00 36.83 C ATOM 3438 O ILE 435 81.434 51.649 −38.588 1.00 36.83 O ATOM 3439 N LYS 436 79.638 52.955 −38.800 1.00 36.83 N ATOM 3440 CA LYS 436 80.269 54.066 −38.100 1.00 36.83 C ATOM 3441 CB LYS 436 79.300 55.241 −37.999 1.00 36.83 C ATOM 3442 CG LYS 436 79.754 56.508 −38.728 1.00 36.83 C ATOM 3443 CD LYS 436 80.906 57.202 −37.998 1.00 36.83 C ATOM 3444 CE LYS 436 80.526 57.598 −36.565 1.00 36.83 C ATOM 3445 NZ LYS 436 81.617 58.321 −35.824 1.00 36.83 N ATOM 3446 C LYS 436 80.652 53.572 −36.699 1.00 36.83 C ATOM 3447 O LYS 436 81.721 53.895 −36.194 1.00 36.83 O ATOM 3448 N ILE 437 79.792 52.770 −36.074 1.00 36.83 N ATOM 3449 CA ILE 437 80.099 52.257 −34.744 1.00 36.83 C ATOM 3450 CB ILE 437 78.914 51.480 −34.117 1.00 36.83 C ATOM 3451 CG2 ILE 437 79.315 50.938 −32.760 1.00 36.83 C ATOM 3452 CG1 ILE 437 77.685 52.383 −33.978 1.00 36.83 C ATOM 3453 CD1 ILE 437 77.960 53.687 −33.292 1.00 36.83 C ATOM 3454 C ILE 437 81.284 51.300 −34.819 1.00 36.83 C ATOM 3455 O ILE 437 82.167 51.316 −33.965 1.00 36.83 O ATOM 3456 N ASN 438 81.303 50.473 −35.855 1.00 36.83 N ATOM 3457 CA ASN 438 82.371 49.500 −36.009 1.00 36.83 C ATOM 3458 CB ASN 438 82.050 48.522 −37.147 1.00 36.83 C ATOM 3459 CG ASN 438 81.170 47.346 −36.693 1.00 36.83 C ATOM 3460 OD1 ASN 438 81.366 46.783 −35.614 1.00 36.83 O ATOM 3461 ND2 ASN 438 80.212 46.968 −37.528 1.00 36.83 N ATOM 3462 C ASN 438 83.763 50.114 −36.221 1.00 36.83 C ATOM 3463 O ASN 438 84.735 49.625 −35.654 1.00 36.83 O ATOM 3464 N ASN 439 83.861 51.178 −37.017 1.00 36.83 N ATOM 3465 CA ASN 439 85.159 51.799 −37.281 1.00 36.83 C ATOM 3466 CB ASN 439 85.020 52.890 −38.360 1.00 36.83 C ATOM 3467 CG ASN 439 86.366 53.299 −38.957 1.00 36.83 C ATOM 3468 OD1 ASN 439 87.166 52.442 −39.393 1.00 36.83 O ATOM 3469 ND2 ASN 439 86.627 54.610 −38.991 1.00 36.83 N ATOM 3470 C ASN 439 85.789 52.378 −36.001 1.00 36.83 C ATOM 3471 O ASN 439 87.012 52.411 −35.857 1.00 36.83 O ATOM 3472 N VAL 440 84.948 52.826 −35.076 1.00 36.83 N ATOM 3473 CA VAL 440 85.412 53.383 −33.811 1.00 36.83 C ATOM 3474 CB VAL 440 84.293 54.204 −33.107 1.00 36.83 C ATOM 3475 CG1 VAL 440 84.717 54.568 −31.704 1.00 36.83 C ATOM 3476 CG2 VAL 440 83.972 55.462 −33.904 1.00 36.83 C ATOM 3477 C VAL 440 85.875 52.318 −32.809 1.00 36.83 C ATOM 3478 O VAL 440 86.976 52.408 −32.273 1.00 36.83 O ATOM 3479 N LEU 441 85.019 51.323 −32.567 1.00 36.83 N ATOM 3480 CA LEU 441 85.265 50.261 −31.596 1.00 36.83 C ATOM 3481 CB LEU 441 83.938 49.550 −31.259 1.00 36.83 C ATOM 3482 CG LEU 441 82.839 50.303 −30.495 1.00 36.83 C ATOM 3483 CD1 LEU 441 81.557 49.460 −30.420 1.00 36.83 C ATOM 3484 CD2 LEU 441 83.328 50.603 −29.096 1.00 36.83 C ATOM 3485 C LEU 441 86.283 49.219 −32.011 1.00 36.83 C ATOM 3486 O LEU 441 86.813 48.489 −31.170 1.00 36.83 O ATOM 3487 N CYS 442 86.537 49.141 −33.309 1.00 36.83 N ATOM 3488 CA CYS 442 87.478 48.172 −33.867 1.00 36.83 C ATOM 3489 CB CYS 442 86.788 47.398 −34.995 1.00 36.83 C ATOM 3490 SG CYS 442 86.948 45.599 −34.908 1.00 36.83 S ATOM 3491 C CYS 442 88.685 48.953 −34.423 1.00 36.83 C ATOM 3492 O CYS 442 88.626 49.493 −35.540 1.00 36.83 O ATOM 3493 N GLN 443 89.766 49.010 −33.643 1.00 36.83 N ATOM 3494 CA GLN 443 90.964 49.743 −34.035 1.00 36.83 C ATOM 3495 CB GLN 443 91.285 50.853 −33.026 1.00 36.83 C ATOM 3496 CG GLN 443 90.202 51.902 −32.822 1.00 36.83 C ATOM 3497 CD GLN 443 89.901 52.693 −34.067 1.00 36.83 C ATOM 3498 OE1 GLN 443 89.488 53.843 −33.984 1.00 36.83 O ATOM 3499 NE2 GLN 443 90.087 52.077 −35.234 1.00 36.83 N ATOM 3500 C GLN 443 92.191 48.869 −34.141 1.00 36.83 C ATOM 3501 O GLN 443 93.268 49.373 −34.482 1.00 36.83 O ATOM 3502 N GLU 444 92.056 47.578 −33.842 1.00 36.83 N ATOM 3503 CA GLU 444 93.211 46.694 −33.914 1.00 36.83 C ATOM 3504 CB GLU 444 94.026 46.793 −32.616 1.00 36.83 C ATOM 3505 CG GLU 444 95.326 45.964 −32.624 1.00 36.83 C ATOM 3506 CD GLU 444 96.182 46.252 −33.852 1.00 36.83 C ATOM 3507 OE1 GLU 444 96.273 47.448 −34.235 1.00 36.83 O ATOM 3508 OE2 GLU 444 96.759 45.295 −34.433 1.00 36.83 O ATOM 3509 C GLU 444 92.808 45.249 −34.165 1.00 36.83 C ATOM 3510 O GLU 444 91.701 44.832 −33.821 1.00 36.83 O ATOM 3511 N ARG 445 93.714 44.499 −34.784 1.00 36.83 N ATOM 3512 CA ARG 445 93.488 43.093 −35.098 1.00 36.83 C ATOM 3513 CB ARG 445 94.703 42.519 −35.838 1.00 36.83 C ATOM 3514 CG ARG 445 94.416 41.998 −37.249 1.00 36.83 C ATOM 3515 CD ARG 445 95.667 41.328 −37.855 1.00 36.83 C ATOM 3516 NE ARG 445 95.362 40.465 −39.003 1.00 36.83 N ATOM 3517 CZ ARG 445 94.524 39.428 −38.951 1.00 36.83 C ATOM 3518 NH1 ARG 445 93.907 39.130 −37.809 1.00 36.83 N ATOM 3519 NH2 ARG 445 94.307 38.683 −40.031 1.00 36.83 N ATOM 3520 C ARG 445 93.296 42.350 −33.787 1.00 36.83 C ATOM 3521 O ARG 445 94.156 42.410 −32.914 1.00 36.83 O ATOM 3522 N LYS 446 92.175 41.659 −33.637 1.00 36.83 N ATOM 3523 CA LYS 446 91.939 40.924 −32.409 1.00 36.83 C ATOM 3524 CB LYS 446 90.484 40.434 −32.306 1.00 36.83 C ATOM 3525 CG LYS 446 90.115 39.300 −33.231 1.00 36.83 C ATOM 3526 CD LYS 446 89.882 39.782 −34.665 1.00 36.83 C ATOM 3527 CE LYS 446 89.231 38.687 −35.524 1.00 36.83 C ATOM 3528 NZ LYS 446 89.087 39.053 −36.979 1.00 36.83 N ATOM 3529 C LYS 446 92.868 39.726 −32.376 1.00 36.83 C ATOM 3530 O LYS 446 93.588 39.467 −33.339 1.00 36.83 O ATOM 3531 N ALA 447 92.849 39.010 −31.257 1.00 36.83 N ATOM 3532 CA ALA 447 93.669 37.833 −31.083 1.00 36.83 C ATOM 3533 CB ALA 447 94.629 38.031 −29.905 1.00 36.83 C ATOM 3534 C ALA 447 92.683 36.725 −30.797 1.00 36.83 C ATOM 3535 O ALA 447 92.711 35.674 −31.418 1.00 36.83 O ATOM 3536 N TYR 448 91.801 36.981 −29.842 1.00 36.83 N ATOM 3537 CA TYR 448 90.753 36.031 −29.480 1.00 36.83 C ATOM 3538 CB TYR 448 91.159 35.304 −28.203 1.00 36.83 C ATOM 3539 CG TYR 448 92.438 34.535 −28.386 1.00 36.83 C ATOM 3540 CD1 TYR 448 92.606 33.707 −29.489 1.00 36.83 C ATOM 3541 CE1 TYR 448 93.781 32.987 −29.684 1.00 36.83 C ATOM 3542 CD2 TYR 448 93.483 34.631 −27.467 1.00 36.83 C ATOM 3543 CE2 TYR 448 94.678 33.913 −27.653 1.00 36.83 C ATOM 3544 CZ TYR 448 94.816 33.090 −28.767 1.00 36.83 C ATOM 3545 OH TYR 448 95.976 32.359 −28.986 1.00 36.83 O ATOM 3546 C TYR 448 89.435 36.786 −29.286 1.00 36.83 C ATOM 3547 O TYR 448 89.421 38.021 −29.316 1.00 36.83 O ATOM 3548 N PHE 449 88.326 36.064 −29.118 1.00 36.83 N ATOM 3549 CA PHE 449 87.048 36.726 −28.883 1.00 36.83 C ATOM 3550 CB PHE 449 86.528 37.407 −30.153 1.00 36.83 C ATOM 3551 CG PHE 449 85.839 36.485 −31.117 1.00 36.83 C ATOM 3552 CD1 PHE 449 86.511 35.991 −32.227 1.00 36.83 C ATOM 3553 CD2 PHE 449 84.511 36.118 −30.927 1.00 36.83 C ATOM 3554 CE1 PHE 449 85.868 35.148 −33.133 1.00 36.83 C ATOM 3555 CE2 PHE 449 83.871 35.275 −31.829 1.00 36.83 C ATOM 3556 CZ PHE 449 84.550 34.794 −32.928 1.00 36.83 C ATOM 3557 C PHE 449 85.930 35.862 −28.304 1.00 36.83 C ATOM 3558 O PHE 449 85.918 34.629 −28.439 1.00 36.83 O ATOM 3559 N ILE 450 85.000 36.544 −27.646 1.00 36.83 N ATOM 3560 CA ILE 450 83.820 35.927 −27.055 1.00 36.83 C ATOM 3561 CB ILE 450 83.675 36.263 −25.551 1.00 36.83 C ATOM 3562 CG2 ILE 450 82.436 35.591 −24.987 1.00 36.83 C ATOM 3563 CG1 ILE 450 84.902 35.782 −24.781 1.00 36.83 C ATOM 3564 CD1 ILE 450 84.842 36.059 −23.286 1.00 36.83 C ATOM 3565 C ILE 450 82.657 36.564 −27.809 1.00 36.83 C ATOM 3566 O ILE 450 82.461 37.788 −27.746 1.00 36.83 O ATOM 3567 N GLY 451 81.912 35.749 −28.553 1.00 36.83 N ATOM 3568 CA GLY 451 80.774 36.274 −29.290 1.00 36.83 C ATOM 3569 C GLY 451 79.497 36.234 −28.465 1.00 36.83 C ATOM 3570 O GLY 451 79.235 35.241 −27.782 1.00 36.83 O ATOM 3571 N VAL 452 78.715 37.311 −28.516 1.00 36.83 N ATOM 3572 CA VAL 452 77.451 37.390 −27.782 1.00 36.83 C ATOM 3573 CB VAL 452 77.429 38.601 −26.812 1.00 36.83 C ATOM 3574 CG1 VAL 452 76.187 38.544 −25.934 1.00 36.83 C ATOM 3575 CG2 VAL 452 78.676 38.600 −25.936 1.00 36.83 C ATOM 3576 C VAL 452 76.297 37.527 −28.772 1.00 36.83 C ATOM 3577 O VAL 452 76.199 38.532 −29.468 1.00 36.83 O ATOM 3578 N LEU 453 75.431 36.511 −28.828 1.00 36.83 N ATOM 3579 CA LEU 453 74.281 36.490 −29.744 1.00 36.83 C ATOM 3580 CB LEU 453 74.085 35.085 −30.320 1.00 36.83 C ATOM 3581 CG LEU 453 72.969 34.893 −31.350 1.00 36.83 C ATOM 3582 CD1 LEU 453 73.368 35.561 −32.641 1.00 36.83 C ATOM 3583 CD2 LEU 453 72.725 33.418 −31.599 1.00 36.83 C ATOM 3584 C LEU 453 72.961 36.925 −29.094 1.00 36.83 C ATOM 3585 O LEU 453 72.512 36.305 −28.128 1.00 36.83 O ATOM 3586 N ASP 454 72.349 37.969 −29.658 1.00 36.83 N ATOM 3587 CA ASP 454 71.094 38.531 −29.177 1.00 36.83 C ATOM 3588 CB ASP 454 71.384 39.857 −28.470 1.00 36.83 C ATOM 3589 CG ASP 454 70.123 40.560 −27.991 1.00 36.83 C ATOM 3590 OD1 ASP 454 69.117 39.874 −27.730 1.00 36.83 O ATOM 3591 OD2 ASP 454 70.134 41.798 −27.855 1.00 36.83 O ATOM 3592 C ASP 454 70.118 38.743 −30.348 1.00 36.83 C ATOM 3593 O ASP 454 70.008 39.845 −30.883 1.00 36.83 O ATOM 3594 N ILE 455 69.420 37.682 −30.747 1.00 36.83 N ATOM 3595 CA ILE 455 68.472 37.751 −31.863 1.00 36.83 C ATOM 3596 CB ILE 455 68.335 36.387 −32.608 1.00 36.83 C ATOM 3597 CG2 ILE 455 69.700 35.875 −33.039 1.00 36.83 C ATOM 3598 CG1 ILE 455 67.645 35.366 −31.700 1.00 36.83 C ATOM 3599 CD1 ILE 455 67.364 34.045 −32.367 1.00 36.83 C ATOM 3600 C ILE 455 67.058 38.143 −31.444 1.00 36.83 C ATOM 3601 O ILE 455 66.729 38.136 −30.262 1.00 36.83 O ATOM 3602 N SER 456 66.227 38.482 −32.425 1.00 36.83 N ATOM 3603 CA SER 456 64.833 38.817 −32.141 1.00 36.83 C ATOM 3604 CB SER 456 64.146 39.418 −33.368 1.00 36.83 C ATOM 3605 OG SER 456 64.660 40.701 −33.673 1.00 36.83 O ATOM 3606 C SER 456 64.190 37.480 −31.799 1.00 36.83 C ATOM 3607 O SER 456 64.308 36.528 −32.563 1.00 36.83 O ATOM 3608 N GLY 457 63.534 37.402 −30.651 1.00 36.83 N ATOM 3609 CA GLY 457 62.918 36.153 −30.236 1.00 36.83 C ATOM 3610 C GLY 457 61.703 35.667 −31.013 1.00 36.83 C ATOM 3611 O GLY 457 61.004 36.425 −31.677 1.00 36.83 O ATOM 3612 N PHE 458 61.464 34.369 −30.916 1.00 36.83 N ATOM 3613 CA PHE 458 60.343 33.717 −31.569 1.00 36.83 C ATOM 3614 CB PHE 458 60.252 32.278 −31.050 1.00 36.83 C ATOM 3615 CG PHE 458 59.206 31.445 −31.724 1.00 36.83 C ATOM 3616 CD1 PHE 458 57.901 31.429 −31.252 1.00 36.83 C ATOM 3617 CD2 PHE 458 59.533 30.662 −32.831 1.00 36.83 C ATOM 3618 CE1 PHE 458 56.932 30.646 −31.866 1.00 36.83 C ATOM 3619 CE2 PHE 458 58.569 29.876 −33.451 1.00 36.83 C ATOM 3620 CZ PHE 458 57.262 29.871 −32.962 1.00 36.83 C ATOM 3621 C PHE 458 59.083 34.510 −31.224 1.00 36.83 C ATOM 3622 O PHE 458 58.872 34.882 −30.066 1.00 36.83 O ATOM 3623 N GLU 459 58.259 34.790 −32.225 1.00 36.83 N ATOM 3624 CA GLU 459 57.041 35.557 −31.984 1.00 36.83 C ATOM 3625 CB GLU 459 57.309 37.052 −32.200 1.00 36.83 C ATOM 3626 CG GLU 459 58.015 37.406 −33.510 1.00 36.83 C ATOM 3627 CD GLU 459 58.134 38.918 −33.715 1.00 36.83 C ATOM 3628 OE1 GLU 459 58.520 39.620 −32.762 1.00 36.83 O ATOM 3629 OE2 GLU 459 57.848 39.403 −34.826 1.00 36.83 O ATOM 3630 C GLU 459 55.805 35.162 −32.785 1.00 36.83 C ATOM 3631 O GLU 459 55.901 34.752 −33.936 1.00 36.83 O ATOM 3632 N ILE 460 54.641 35.300 −32.158 1.00 36.83 N ATOM 3633 CA ILE 460 53.388 34.998 −32.823 1.00 36.83 C ATOM 3634 CB ILE 460 52.750 33.683 −32.317 1.00 36.83 C ATOM 3635 CG2 ILE 460 51.510 33.366 −33.141 1.00 36.83 C ATOM 3636 CG1 ILE 460 53.741 32.528 −32.433 1.00 36.83 C ATOM 3637 CD1 ILE 460 53.200 31.214 −31.915 1.00 36.83 C ATOM 3638 C ILE 460 52.380 36.124 −32.589 1.00 36.83 C ATOM 3639 O ILE 460 52.020 36.419 −31.457 1.00 36.83 O ATOM 3640 N PHE 461 51.945 36.745 −33.675 1.00 36.83 N ATOM 3641 CA PHE 461 50.959 37.820 −33.642 1.00 36.83 C ATOM 3642 CB PHE 461 51.495 39.055 −34.359 1.00 36.83 C ATOM 3643 CG PHE 461 52.752 39.612 −33.767 1.00 36.83 C ATOM 3644 CD1 PHE 461 52.784 40.054 −32.454 1.00 36.83 C ATOM 3645 CD2 PHE 461 53.896 39.735 −34.540 1.00 36.83 C ATOM 3646 CE1 PHE 461 53.947 40.617 −31.921 1.00 36.83 C ATOM 3647 CE2 PHE 461 55.057 40.297 −34.014 1.00 36.83 C ATOM 3648 CZ PHE 461 55.082 40.738 −32.704 1.00 36.83 C ATOM 3649 C PHE 461 49.715 37.342 −34.395 1.00 36.83 C ATOM 3650 O PHE 461 49.693 36.228 −34.919 1.00 36.83 O ATOM 3651 N LYS 462 48.698 38.202 −34.464 1.00 36.83 N ATOM 3652 CA LYS 462 47.467 37.884 −35.180 1.00 36.83 C ATOM 3653 CB LYS 462 46.442 39.016 −35.048 1.00 36.83 C ATOM 3654 CG LYS 462 45.819 39.148 −33.669 1.00 36.83 C ATOM 3655 CD LYS 462 45.580 40.623 −33.308 1.00 36.83 C ATOM 3656 CE LYS 462 44.852 41.405 −34.422 1.00 36.83 C ATOM 3657 NZ LYS 462 45.728 41.753 −35.610 1.00 36.83 N ATOM 3658 C LYS 462 47.840 37.712 −36.638 1.00 36.83 C ATOM 3659 O LYS 462 47.379 36.793 −37.296 1.00 36.83 O ATOM 3660 N VAL 463 48.666 38.622 −37.136 1.00 36.83 N ATOM 3661 CA VAL 463 49.131 38.564 −38.516 1.00 36.83 C ATOM 3662 CB VAL 463 48.806 39.869 −39.309 1.00 36.83 C ATOM 3663 CG1 VAL 463 49.024 39.644 −40.784 1.00 36.83 C ATOM 3664 CG2 VAL 463 47.376 40.302 −39.062 1.00 36.83 C ATOM 3665 C VAL 463 50.652 38.387 −38.495 1.00 36.83 C ATOM 3666 O VAL 463 51.375 39.224 −37.939 1.00 36.83 O ATOM 3667 N ASN 464 51.117 37.287 −39.079 1.00 36.83 N ATOM 3668 CA ASN 464 52.540 36.986 −39.184 1.00 36.83 C ATOM 3669 CB ASN 464 52.844 35.599 −38.623 1.00 36.83 C ATOM 3670 CG ASN 464 52.426 35.461 −37.185 1.00 36.83 C ATOM 3671 OD1 ASN 464 52.874 36.218 −36.336 1.00 36.83 O ATOM 3672 ND2 ASN 464 51.561 34.501 −36.903 1.00 36.83 N ATOM 3673 C ASN 464 52.871 37.022 −40.663 1.00 36.83 C ATOM 3674 O ASN 464 52.253 36.327 −41.467 1.00 36.83 O ATOM 3675 N SER 465 53.836 37.845 −41.027 1.00 36.83 N ATOM 3676 CA SER 465 54.224 37.974 −42.420 1.00 36.83 C ATOM 3677 CB SER 465 54.124 39.448 −42.832 1.00 36.83 C ATOM 3678 OG SER 465 54.317 39.615 −44.220 1.00 36.83 O ATOM 3679 C SER 465 55.645 37.421 −42.651 1.00 36.83 C ATOM 3680 O SER 465 56.154 36.651 −41.846 1.00 36.83 O ATOM 3681 N PHE 466 56.259 37.823 −43.758 1.00 36.83 N ATOM 3682 CA PHE 466 57.588 37.371 −44.134 1.00 36.83 C ATOM 3683 CB PHE 466 58.019 38.041 −45.448 1.00 36.83 C ATOM 3684 CG PHE 466 59.355 37.578 −45.957 1.00 36.83 C ATOM 3685 CD1 PHE 466 59.598 36.227 −46.198 1.00 36.83 C ATOM 3686 CD2 PHE 466 60.368 38.496 −46.223 1.00 36.83 C ATOM 3687 CE1 PHE 466 60.829 35.804 −46.699 1.00 36.83 C ATOM 3688 CE2 PHE 466 61.604 38.077 −46.726 1.00 36.83 C ATOM 3689 CZ PHE 466 61.830 36.730 −46.963 1.00 36.83 C ATOM 3690 C PHE 466 58.625 37.629 −43.048 1.00 36.83 C ATOM 3691 O PHE 466 59.504 36.807 −42.830 1.00 36.83 O ATOM 3692 N GLU 467 58.510 38.772 −42.381 1.00 36.83 N ATOM 3693 CA GLU 467 59.417 39.134 −41.298 1.00 36.83 C ATOM 3694 CB GLU 467 59.011 40.497 −40.712 1.00 36.83 C ATOM 3695 CG GLU 467 59.346 41.686 −41.616 1.00 36.83 C ATOM 3696 CD GLU 467 58.269 42.015 −42.649 1.00 36.83 C ATOM 3697 OE1 GLU 467 57.386 41.159 −42.926 1.00 36.83 O ATOM 3698 OE2 GLU 467 58.324 43.145 −43.192 1.00 36.83 O ATOM 3699 C GLU 467 59.413 38.059 −40.195 1.00 36.83 C ATOM 3700 O GLU 467 60.475 37.596 −39.765 1.00 36.83 O ATOM 3701 N GLN 468 58.213 37.667 −39.762 1.00 36.83 N ATOM 3702 CA GLN 468 58.020 36.656 −38.729 1.00 36.83 C ATOM 3703 CB GLN 468 56.529 36.497 −38.402 1.00 36.83 C ATOM 3704 CG GLN 468 55.946 37.577 −37.503 1.00 36.83 C ATOM 3705 CD GLN 468 56.009 38.963 −38.111 1.00 36.83 C ATOM 3706 OE1 GLN 468 55.456 39.217 −39.176 1.00 36.83 O ATOM 3707 NE2 GLN 468 56.686 39.868 −37.432 1.00 36.83 N ATOM 3708 C GLN 468 58.593 35.294 −39.116 1.00 36.83 C ATOM 3709 O GLN 468 59.136 34.591 −38.271 1.00 36.83 O ATOM 3710 N LEU 469 58.447 34.908 −40.381 1.00 36.83 N ATOM 3711 CA LEU 469 58.992 33.632 −40.846 1.00 36.83 C ATOM 3712 CB LEU 469 58.621 33.380 −42.309 1.00 36.83 C ATOM 3713 CG LEU 469 59.250 32.108 −42.880 1.00 36.83 C ATOM 3714 CD1 LEU 469 58.763 30.935 −42.081 1.00 36.83 C ATOM 3715 CD2 LEU 469 58.903 31.939 −44.351 1.00 36.83 C ATOM 3716 C LEU 469 60.523 33.661 −40.704 1.00 36.83 C ATOM 3717 O LEU 469 61.127 32.736 −40.182 1.00 36.83 O ATOM 3718 N CYS 470 61.141 34.739 −41.165 1.00 36.83 N ATOM 3719 CA CYS 470 62.586 34.888 −41.063 1.00 36.83 C ATOM 3720 CB CYS 470 63.022 36.202 −41.710 1.00 36.83 C ATOM 3721 SG CYS 470 62.819 36.239 −43.490 1.00 36.83 S ATOM 3722 C CYS 470 63.019 34.856 −39.598 1.00 36.83 C ATOM 3723 O CYS 470 64.008 34.233 −39.253 1.00 36.83 O ATOM 3724 N ILE 471 62.262 35.524 −38.736 1.00 36.83 N ATOM 3725 CA ILE 471 62.581 35.545 −37.315 1.00 36.83 C ATOM 3726 CB ILE 471 61.648 36.511 −36.540 1.00 36.83 C ATOM 3727 CG2 ILE 471 61.851 36.354 −35.006 1.00 36.83 C ATOM 3728 CG1 ILE 471 61.883 37.946 −37.014 1.00 36.83 C ATOM 3729 CD1 ILE 471 60.876 38.922 −36.459 1.00 36.83 C ATOM 3730 C ILE 471 62.451 34.156 −36.706 1.00 36.83 C ATOM 3731 O ILE 471 63.388 33.657 −36.098 1.00 36.83 O ATOM 3732 N ASN 472 61.292 33.531 −36.881 1.00 36.83 N ATOM 3733 CA ASN 472 61.037 32.209 −36.306 1.00 36.83 C ATOM 3734 CB ASN 472 59.561 31.829 −36.504 1.00 36.83 C ATOM 3735 CG ASN 472 58.625 32.617 −35.578 1.00 36.83 C ATOM 3736 OD1 ASN 472 57.392 32.568 −35.712 1.00 36.83 O ATOM 3737 ND2 ASN 472 59.207 33.337 −34.634 1.00 36.83 N ATOM 3738 C ASN 472 61.964 31.118 −36.832 1.00 36.83 C ATOM 3739 O ASN 472 62.256 30.150 −36.130 1.00 36.83 O ATOM 3740 N TYR 473 62.417 31.293 −38.072 1.00 36.83 N ATOM 3741 CA TYR 473 63.340 30.378 −38.729 1.00 36.83 C ATOM 3742 CB TYR 473 63.462 30.761 −40.208 1.00 36.83 C ATOM 3743 CG TYR 473 64.707 30.263 −40.920 1.00 36.83 C ATOM 3744 CD1 TYR 473 64.973 28.895 −41.053 1.00 36.83 C ATOM 3745 CE1 TYR 473 66.085 28.450 −41.767 1.00 36.83 C ATOM 3746 CD2 TYR 473 65.590 31.166 −41.517 1.00 36.83 C ATOM 3747 CE2 TYR 473 66.699 30.727 −42.236 1.00 36.83 C ATOM 3748 CZ TYR 473 66.939 29.376 −42.355 1.00 36.83 C ATOM 3749 OH TYR 473 68.023 28.959 −43.068 1.00 36.83 O ATOM 3750 C TYR 473 64.699 30.480 −38.037 1.00 36.83 C ATOM 3751 O TYR 473 65.370 29.474 −37.821 1.00 36.83 O ATOM 3752 N THR 474 65.086 31.704 −37.684 1.00 36.83 N ATOM 3753 CA THR 474 66.358 31.942 −37.009 1.00 36.83 O ATOM 3754 CB THR 474 66.658 33.459 −36.845 1.00 36.83 C ATOM 3755 OG1 THR 474 66.640 34.103 −38.120 1.00 36.83 O ATOM 3756 CG2 THR 474 68.018 33.667 −36.225 1.00 36.83 C ATOM 3757 C THR 474 66.313 31.299 −35.624 1.00 36.83 C ATOM 3758 O THR 474 67.288 30.687 −35.177 1.00 36.83 O ATOM 3759 N ASN 475 65.168 31.434 −34.960 1.00 36.83 N ATOM 3760 CA ASN 475 64.995 30.873 −33.632 1.00 36.83 C ATOM 3761 CB ASN 475 63.694 31.389 −33.001 1.00 36.83 C ATOM 3762 CG ASN 475 63.833 32.792 −32.453 1.00 36.83 C ATOM 3763 OD1 ASN 475 64.089 32.972 −31.277 1.00 36.83 O ATOM 3764 ND2 ASN 475 63.683 33.789 −33.312 1.00 36.83 N ATOM 3765 C ASN 475 64.999 29.353 −33.681 1.00 36.83 C ATOM 3766 O ASN 475 65.402 28.709 −32.720 1.00 36.83 O ATOM 3767 N GLU 476 64.557 28.792 −34.806 1.00 36.83 N ATOM 3768 CA GLU 476 64.533 27.344 −34.977 1.00 36.83 C ATOM 3769 CB GLU 476 63.644 26.956 −36.157 1.00 36.83 C ATOM 3770 CG GLU 476 63.399 25.459 −36.270 1.00 36.83 C ATOM 3771 CD GLU 476 62.060 25.019 −35.686 1.00 36.83 C ATOM 3772 OE1 GLU 476 61.977 23.889 −35.178 1.00 36.83 O ATOM 3773 OE2 GLU 476 61.087 25.789 −35.737 1.00 36.83 O ATOM 3774 C GLU 476 65.969 26.825 −35.210 1.00 36.83 C ATOM 3775 O GLU 476 66.323 25.736 −34.751 1.00 36.83 O ATOM 3776 N LYS 477 66.789 27.600 −35.919 1.00 36.83 N ATOM 3777 CA LYS 477 68.167 27.184 −36.151 1.00 36.83 C ATOM 3778 CB LYS 477 68.816 28.009 −37.256 1.00 36.83 C ATOM 3779 CG LYS 477 68.184 27.756 −38.606 1.00 36.83 C ATOM 3780 CD LYS 477 69.132 28.016 −39.761 1.00 36.83 C ATOM 3781 CE LYS 477 70.227 26.963 −39.850 1.00 36.83 C ATOM 3782 NZ LYS 477 70.761 26.860 −41.247 1.00 36.83 N ATOM 3783 C LYS 477 68.991 27.264 −34.861 1.00 36.83 C ATOM 3784 O LYS 477 69.775 26.376 −34.576 1.00 36.83 O ATOM 3785 N LEU 478 68.787 28.315 −34.073 1.00 36.83 N ATOM 3786 CA LEU 478 69.497 28.451 −32.813 1.00 36.83 C ATOM 3787 CB LEU 478 69.146 29.784 −32.159 1.00 36.83 C ATOM 3788 CG LEU 478 69.755 30.124 −30.793 1.00 36.83 C ATOM 3789 CD1 LEU 478 71.224 29.782 −30.745 1.00 36.83 C ATOM 3790 CD2 LEU 478 69.539 31.596 −30.525 1.00 36.83 C ATOM 3791 C LEU 478 69.152 27.277 −31.878 1.00 36.83 C ATOM 3792 O LEU 478 70.034 26.723 −31.208 1.00 36.83 O ATOM 3793 N GLN 479 67.874 26.899 −31.837 1.00 36.83 N ATOM 3794 CA GLN 479 67.459 25.780 −31.006 1.00 36.83 C ATOM 3795 CB GLN 479 65.935 25.654 −30.982 1.00 36.83 C ATOM 3796 CG GLN 479 65.420 24.409 −30.289 1.00 36.83 C ATOM 3797 CD GLN 479 65.781 24.346 −28.812 1.00 36.83 C ATOM 3798 OE1 GLN 479 65.536 25.285 −28.060 1.00 36.83 O ATOM 3799 NE2 GLN 479 66.350 23.220 −28.389 1.00 36.83 N ATOM 3800 C GLN 479 68.077 24.474 −31.509 1.00 36.83 C ATOM 3801 O GLN 479 68.394 23.590 −30.720 1.00 36.83 O ATOM 3802 N GLN 480 68.237 24.337 −32.818 1.00 36.83 N ATOM 3803 CA GLN 480 68.847 23.128 −33.354 1.00 36.83 C ATOM 3804 CB GLN 480 68.702 23.064 −34.866 1.00 36.83 C ATOM 3805 CG GLN 480 69.062 21.708 −35.458 1.00 36.83 C ATOM 3806 CD GLN 480 68.157 20.594 −34.957 1.00 36.83 C ATOM 3807 OE1 GLN 480 67.863 19.650 −35.682 1.00 36.83 O ATOM 3808 NE2 GLN 480 67.724 20.691 −33.719 1.00 36.83 N ATOM 3809 C GLN 480 70.330 23.111 −32.974 1.00 36.83 C ATOM 3810 O GLN 480 70.897 22.061 −32.696 1.00 36.83 O ATOM 3811 N PHE 481 70.945 24.285 −32.968 1.00 36.83 N ATOM 3812 CA PHE 481 72.336 24.411 −32.582 1.00 36.83 C ATOM 3813 CB PHE 481 72.770 25.873 −32.633 1.00 36.83 C ATOM 3814 CG PHE 481 74.236 26.071 −32.424 1.00 36.83 C ATOM 3815 CD1 PHE 481 75.137 25.728 −33.415 1.00 36.83 C ATOM 3816 CD2 PHE 481 74.714 26.608 −31.242 1.00 36.83 C ATOM 3817 CE1 PHE 481 76.506 25.921 −33.241 1.00 36.83 C ATOM 3818 CE2 PHE 481 76.077 26.804 −31.053 1.00 36.83 C ATOM 3819 CZ PHE 481 76.977 26.459 −32.062 1.00 36.83 C ATOM 3820 C PHE 481 72.450 23.880 −31.141 1.00 36.83 C ATOM 3821 O PHE 481 73.349 23.108 −30.829 1.00 36.83 O ATOM 3822 N PHE 482 71.531 24.289 −30.271 1.00 36.83 N ATOM 3823 CA PHE 482 71.543 23.812 −28.896 1.00 36.83 C ATOM 3824 CB PHE 482 70.345 24.361 −28.130 1.00 36.83 C ATOM 3825 CG PHE 482 70.238 23.866 −26.706 1.00 36.83 C ATOM 3826 CD1 PHE 482 71.018 24.422 −25.697 1.00 36.83 C ATOM 3827 CD2 PHE 482 69.321 22.874 −26.369 1.00 36.83 C ATOM 3828 CE1 PHE 482 70.877 23.999 −24.373 1.00 36.83 C ATOM 3829 CE2 PHE 482 69.175 22.444 −25.053 1.00 36.83 C ATOM 3830 CZ PHE 482 69.949 23.004 −24.053 1.00 36.83 C ATOM 3831 C PHE 482 71.466 22.292 −28.930 1.00 36.83 C ATOM 3832 O PHE 482 72.282 21.605 −28.304 1.00 36.83 O ATOM 3833 N ASN 483 70.483 21.771 −29.665 1.00 36.83 N ATOM 3834 CA ASN 483 70.299 20.327 −29.782 1.00 36.83 C ATOM 3835 CB ASN 483 69.176 20.000 −30.776 1.00 36.83 C ATOM 3836 CG ASN 483 67.807 20.552 −30.342 1.00 36.83 C ATOM 3837 OD1 ASN 483 67.502 20.625 −29.158 1.00 36.83 O ATOM 3838 ND2 ASN 483 66.980 20.921 −31.312 1.00 36.83 N ATOM 3839 C ASN 483 71.591 19.631 −30.234 1.00 36.83 C ATOM 3840 O ASN 483 71.953 18.566 −29.736 1.00 36.83 O ATOM 3841 N HIS 484 72.278 20.248 −31.180 1.00 36.83 N ATOM 3842 CA HIS 484 73.507 19.693 −31.725 1.00 36.83 C ATOM 3843 CB HIS 484 73.992 20.591 −32.870 1.00 36.83 C ATOM 3844 CG HIS 484 74.996 19.944 −33.771 1.00 36.83 C ATOM 3845 CD2 HIS 484 76.175 20.395 −34.262 1.00 36.83 C ATOM 3846 ND1 HIS 484 74.808 18.692 −34.316 1.00 36.83 N ATOM 3847 CE1 HIS 484 75.824 18.399 −35.106 1.00 36.83 C ATOM 3848 NE2 HIS 484 76.667 19.417 −35.091 1.00 36.83 N ATOM 3849 C HIS 484 74.606 19.529 −30.658 1.00 36.83 C ATOM 3850 O HIS 484 75.104 18.417 −30.436 1.00 36.83 O ATOM 3851 N HIS 485 74.960 20.627 −29.997 1.00 36.83 N ATOM 3852 CA HIS 485 75.995 20.617 −28.968 1.00 36.83 C ATOM 3853 CB HIS 485 76.474 22.046 −28.718 1.00 36.83 C ATOM 3854 CG HIS 485 77.201 22.642 −29.883 1.00 36.83 C ATOM 3855 CD2 HIS 485 76.748 23.340 −30.956 1.00 36.83 C ATOM 3856 ND1 HIS 485 78.561 22.498 −30.068 1.00 36.83 N ATOM 3857 CE1 HIS 485 78.914 23.081 −31.200 1.00 36.83 C ATOM 3858 NE2 HIS 485 77.834 23.598 −31.761 1.00 36.83 N ATOM 3859 C HIS 485 75.660 19.942 −27.632 1.00 36.83 C ATOM 3860 O HIS 485 76.574 19.624 −26.872 1.00 36.83 O ATOM 3861 N MET 486 74.380 19.708 −27.342 1.00 36.83 N ATOM 3862 CA MET 486 73.992 19.066 −26.083 1.00 36.83 C ATOM 3863 CB MET 486 72.686 19.657 −25.556 1.00 36.83 C ATOM 3864 CG MET 486 72.835 21.029 −24.953 1.00 36.83 C ATOM 3865 SD MET 486 73.916 20.969 −23.538 1.00 36.83 S ATOM 3866 CE MET 486 72.835 20.223 −22.333 1.00 36.83 C ATOM 3867 C MET 486 73.803 17.567 −26.226 1.00 36.83 C ATOM 3868 O MET 486 74.160 16.784 −25.340 1.00 36.83 O ATOM 3869 N PHE 487 73.231 17.174 −27.351 1.00 36.83 N ATOM 3870 CA PHE 487 72.975 15.776 −27.597 1.00 36.83 C ATOM 3871 CB PHE 487 71.491 15.593 −27.920 1.00 36.83 C ATOM 3872 CG PHE 487 70.590 16.420 −27.042 1.00 36.83 C ATOM 3873 CD1 PHE 487 70.633 16.280 −25.652 1.00 36.83 C ATOM 3874 CD2 PHE 487 69.760 17.389 −27.591 1.00 36.83 C ATOM 3875 CE1 PHE 487 69.867 17.104 −24.814 1.00 36.83 C ATOM 3876 CE2 PHE 487 68.983 18.225 −26.763 1.00 36.83 C ATOM 3877 CZ PHE 487 69.042 18.081 −25.369 1.00 36.83 C ATOM 3878 C PHE 487 73.861 15.261 −28.710 1.00 36.83 C ATOM 3879 O PHE 487 74.886 14.653 −28.440 1.00 36.83 O ATOM 3880 N LYS 488 73.494 15.531 −29.952 1.00 36.83 N ATOM 3881 CA LYS 488 74.260 15.062 −31.103 1.00 36.83 C ATOM 3882 CB LYS 488 73.976 15.959 −32.316 1.00 36.83 C ATOM 3883 CG LYS 488 74.406 15.372 −33.663 1.00 36.83 C ATOM 3884 CD LYS 488 73.762 14.011 −33.897 1.00 36.83 C ATOM 3885 CE LYS 488 73.604 13.703 −35.391 1.00 36.83 C ATOM 3886 NZ LYS 488 74.876 13.794 −36.139 1.00 36.83 N ATOM 3887 C LYS 488 75.775 14.978 −30.846 1.00 36.83 C ATOM 3888 O LYS 488 76.285 13.926 −30.462 1.00 36.83 O ATOM 3889 N LEU 489 76.496 16.077 −31.048 1.00 36.83 N ATOM 3890 CA LEU 489 77.947 16.061 −30.839 1.00 36.83 C ATOM 3891 CB LEU 489 78.507 17.492 −30.755 1.00 36.83 C ATOM 3892 CG LEU 489 78.385 18.329 −32.023 1.00 36.83 C ATOM 3893 CD1 LEU 489 79.219 19.586 −31.892 1.00 36.83 C ATOM 3894 CD2 LEU 489 78.863 17.512 −33.206 1.00 36.83 C ATOM 3895 C LEU 489 78.362 15.282 −29.589 1.00 36.83 C ATOM 3896 O LEU 489 79.264 14.453 −29.639 1.00 36.83 O ATOM 3897 N GLU 490 77.699 15.549 −28.475 1.00 36.83 N ATOM 3898 CA GLU 490 78.021 14.885 −27.219 1.00 36.83 C ATOM 3899 CB GLU 490 76.988 15.259 −26.160 1.00 36.83 C ATOM 3900 CG GLU 490 77.251 14.680 −24.792 1.00 36.83 C ATOM 3901 CD GLU 490 78.647 14.990 −24.294 1.00 36.83 C ATOM 3902 OE1 GLU 490 79.285 15.930 −24.826 1.00 36.83 O ATOM 3903 OE2 GLU 490 79.097 14.298 −23.355 1.00 36.83 O ATOM 3904 C GLU 490 78.079 13.369 −27.357 1.00 36.83 C ATOM 3905 O GLU 490 79.084 12.736 −27.027 1.00 36.83 O ATOM 3906 N GLN 491 76.996 12.790 −27.854 1.00 36.83 N ATOM 3907 CA GLN 491 76.914 11.351 −28.007 1.00 36.83 C ATOM 3908 CB GLN 491 75.485 10.935 −28.334 1.00 36.83 C ATOM 3909 CG GLN 491 74.464 11.240 −27.260 1.00 36.83 C ATOM 3910 CD GLN 491 73.212 10.388 −27.418 1.00 36.83 C ATOM 3911 OE1 GLN 491 73.106 9.316 −26.834 1.00 36.83 O ATOM 3912 NE2 GLN 491 72.272 10.853 −28.232 1.00 36.83 N ATOM 3913 C GLN 491 77.847 10.799 −29.064 1.00 36.83 C ATOM 3914 O GLN 491 78.481 9.767 −28.854 1.00 36.83 O ATOM 3915 N GLU 492 77.936 11.474 −30.205 1.00 36.83 N ATOM 3916 CA GLU 492 78.800 10.995 −31.271 1.00 36.83 C ATOM 3917 CB GLU 492 78.772 11.935 −32.452 1.00 36.83 C ATOM 3918 CG GLU 492 77.470 11.981 −33.184 1.00 36.83 C ATOM 3919 CD GLU 492 77.510 13.079 −34.218 1.00 36.83 C ATOM 3920 OE1 GLU 492 78.074 14.146 −33.871 1.00 36.83 O ATOM 3921 OE2 GLU 492 77.000 12.877 −35.352 1.00 36.83 O ATOM 3922 C GLU 492 80.236 10.823 −30.827 1.00 36.83 C ATOM 3923 O GLU 492 80.995 10.083 −31.454 1.00 36.83 O ATOM 3924 N GLU 493 80.603 11.524 −29.761 1.00 36.83 N ATOM 3925 CA GLU 493 81.942 11.464 −29.201 1.00 36.83 C ATOM 3926 CB GLU 493 82.180 12.715 −28.346 1.00 36.83 C ATOM 3927 CG GLU 493 83.554 12.830 −27.676 1.00 36.83 C ATOM 3928 CD GLU 493 84.710 12.898 −28.672 1.00 36.83 C ATOM 3929 OE1 GLU 493 84.735 13.817 −29.522 1.00 36.83 O ATOM 3930 OE2 GLU 493 85.603 12.032 −28.600 1.00 36.83 O ATOM 3931 C GLU 493 81.995 10.197 −28.334 1.00 36.83 C ATOM 3932 O GLU 493 83.046 9.551 −28.198 1.00 36.83 O ATOM 3933 N TYR 494 80.844 9.842 −27.765 1.00 36.83 N ATOM 3934 CA TYR 494 80.746 8.675 −26.917 1.00 36.83 C ATOM 3935 CB TYR 494 79.374 8.577 −26.269 1.00 36.83 C ATOM 3936 CG TYR 494 79.125 9.525 −25.131 1.00 36.83 C ATOM 3937 CD1 TYR 494 80.164 9.962 −24.312 1.00 36.83 C ATOM 3938 CE1 TYR 494 79.914 10.822 −23.246 1.00 36.83 C ATOM 3939 CD2 TYR 494 77.835 9.964 −24.857 1.00 36.83 C ATOM 3940 CE2 TYR 494 77.580 10.814 −23.807 1.00 36.83 C ATOM 3941 CZ TYR 494 78.614 11.245 −23.008 1.00 36.83 C ATOM 3942 OH TYR 494 78.333 12.138 −22.003 1.00 36.83 O ATOM 3943 C TYR 494 80.978 7.387 −27.669 1.00 36.83 C ATOM 3944 O TYR 494 81.842 6.588 −27.288 1.00 36.83 O ATOM 3945 N LEU 495 80.184 7.181 −28.715 1.00 36.83 N ATOM 3946 CA LEU 495 80.250 5.963 −29.515 1.00 36.83 C ATOM 3947 CB LEU 495 78.876 5.656 −30.115 1.00 36.83 C ATOM 3948 CG LEU 495 77.724 5.388 −29.137 1.00 36.83 C ATOM 3949 CD1 LEU 495 76.455 5.236 −29.945 1.00 36.83 C ATOM 3950 CD2 LEU 495 77.987 4.150 −28.286 1.00 36.83 C ATOM 3951 C LEU 495 81.285 6.024 −30.624 1.00 36.83 C ATOM 3952 O LEU 495 81.126 5.406 −31.687 1.00 36.83 O ATOM 3953 N LYS 496 82.332 6.799 −30.371 1.00 36.83 N ATOM 3954 CA LYS 496 83.440 6.971 −31.306 1.00 36.83 C ATOM 3955 CB LYS 496 83.528 8.432 −31.754 1.00 36.83 C ATOM 3956 CG LYS 496 84.892 8.860 −32.313 1.00 36.83 C ATOM 3957 CD LYS 496 84.955 8.767 −33.836 1.00 36.83 C ATOM 3958 CE LYS 496 86.317 9.218 −34.333 1.00 36.83 C ATOM 3959 NZ LYS 496 87.388 8.302 −33.805 1.00 36.83 N ATOM 3960 C LYS 496 84.640 6.610 −30.457 1.00 36.83 C ATOM 3961 O LYS 496 85.748 6.372 −30.960 1.00 36.83 O ATOM 3962 N GLU 497 84.388 6.564 −29.153 1.00 36.83 N ATOM 3963 CA GLU 497 85.403 6.240 −28.173 1.00 36.83 C ATOM 3964 CB GLU 497 85.598 7.431 −27.255 1.00 36.83 C ATOM 3965 CG GLU 497 86.224 8.580 −28.024 1.00 36.83 C ATOM 3966 CD GLU 497 87.479 8.121 −28.740 1.00 36.83 C ATOM 3967 OE1 GLU 497 88.373 7.610 −28.029 1.00 36.83 O ATOM 3968 OE2 GLU 497 87.574 8.259 −29.994 1.00 36.83 O ATOM 3969 C GLU 497 85.123 4.974 −27.376 1.00 36.83 C ATOM 3970 O GLU 497 85.680 4.784 −26.285 1.00 36.83 O ATOM 3971 N LYS 498 84.261 4.116 −27.929 1.00 36.83 N ATOM 3972 CA LYS 498 83.928 2.823 −27.318 1.00 36.83 C ATOM 3973 CB LYS 498 84.963 1.771 −27.748 1.00 36.83 C ATOM 3974 CG LYS 498 85.111 1.615 −29.258 1.00 36.83 C ATOM 3975 CD LYS 498 83.811 1.176 −29.906 1.00 36.83 C ATOM 3976 CE LYS 498 83.845 1.433 −31.404 1.00 36.83 C ATOM 3977 NZ LYS 498 83.993 2.894 −31.737 1.00 36.83 N ATOM 3978 C LYS 498 83.877 2.899 −25.796 1.00 36.83 C ATOM 3979 O LYS 498 84.726 2.337 −25.083 1.00 36.83 O ATOM 3980 N ILE 499 82.857 3.589 −25.318 1.00 36.83 N ATOM 3981 CA ILE 499 82.619 3.815 −23.905 1.00 36.83 C ATOM 3982 CB ILE 499 82.393 5.358 −23.701 1.00 36.83 C ATOM 3983 CG2 ILE 499 81.492 5.661 −22.523 1.00 36.83 C ATOM 3984 CG1 ILE 499 83.753 6.044 −23.526 1.00 36.83 C ATOM 3985 CD1 ILE 499 84.458 5.706 −22.202 1.00 36.83 C ATOM 3986 C ILE 499 81.396 2.974 −23.533 1.00 36.83 C ATOM 3987 O ILE 499 80.778 3.156 −22.478 1.00 36.83 O ATOM 3988 N ASN 500 81.076 2.018 −24.401 1.00 36.83 N ATOM 3989 CA ASN 500 79.904 1.185 −24.188 1.00 36.83 C ATOM 3990 CB ASN 500 80.205 0.034 −23.222 1.00 36.83 C ATOM 3991 CG ASN 500 81.081 −1.037 −23.857 1.00 36.83 C ATOM 3992 OD1 ASN 500 80.706 −1.643 −24.875 1.00 36.83 O ATOM 3993 ND2 ASN 500 82.257 −1.274 −23.265 1.00 36.83 N ATOM 3994 C ASN 500 78.777 2.043 −23.632 1.00 36.83 C ATOM 3995 O ASN 500 78.396 1.913 −22.472 1.00 36.83 O ATOM 3996 N TRP 501 78.258 2.929 −24.475 1.00 36.83 N ATOM 3997 CA TRP 501 77.164 3.820 −24.101 1.00 36.83 C ATOM 3998 CB TRP 501 77.592 5.275 −24.313 1.00 36.83 C ATOM 3999 CG TRP 501 76.474 6.271 −24.532 1.00 36.83 C ATOM 4000 CD2 TRP 501 75.897 7.152 −23.550 1.00 36.83 C ATOM 4001 CE2 TRP 501 74.928 7.940 −24.213 1.00 36.83 C ATOM 4002 CE3 TRP 501 76.110 7.354 −22.179 1.00 36.83 C ATOM 4003 CD1 TRP 501 75.841 6.551 −25.715 1.00 36.83 C ATOM 4004 NE1 TRP 501 74.913 7.555 −25.530 1.00 36.83 N ATOM 4005 CZ2 TRP 501 74.175 8.913 −23.550 1.00 36.83 C ATOM 4006 CZ3 TRP 501 75.357 8.327 −21.519 1.00 36.83 C ATOM 4007 CH2 TRP 501 74.403 9.092 −22.209 1.00 36.83 C ATOM 4008 C TRP 501 75.985 3.484 −24.981 1.00 36.83 C ATOM 4009 O TRP 501 76.151 3.337 −26.186 1.00 36.83 O ATOM 4010 N THR 502 74.800 3.338 −24.385 1.00 36.83 N ATOM 4011 CA THR 502 73.616 3.022 −25.171 1.00 36.83 C ATOM 4012 CB THR 502 72.575 2.209 −24.355 1.00 36.83 C ATOM 4013 OG1 THR 502 71.756 3.090 −23.565 1.00 36.83 O ATOM 4014 CG2 THR 502 73.298 1.223 −23.431 1.00 36.83 C ATOM 4015 C THR 502 72.996 4.330 −25.646 1.00 36.83 C ATOM 4016 O THR 502 72.483 5.119 −24.843 1.00 36.83 O ATOM 4017 N PHE 503 73.082 4.562 −26.952 1.00 36.83 N ATOM 4018 CA PHE 503 72.534 5.768 −27.559 1.00 36.83 C ATOM 4019 CB PHE 503 72.490 5.598 −29.082 1.00 36.83 C ATOM 4020 CG PHE 503 71.674 6.645 −29.793 1.00 36.83 C ATOM 4021 CD1 PHE 503 72.244 7.857 −30.164 1.00 36.83 C ATOM 4022 CD2 PHE 503 70.338 6.417 −30.083 1.00 36.83 C ATOM 4023 CE1 PHE 503 71.493 8.825 −30.812 1.00 36.83 C ATOM 4024 CE2 PHE 503 69.567 7.383 −30.734 1.00 36.83 C ATOM 4025 CZ PHE 503 70.148 8.588 −31.098 1.00 36.83 C ATOM 4026 C PHE 503 71.126 6.059 −27.018 1.00 36.83 C ATOM 4027 O PHE 503 70.350 5.141 −26.705 1.00 36.83 O ATOM 4028 N ILE 504 70.799 7.338 −26.895 1.00 36.83 N ATOM 4029 CA ILE 504 69.484 7.718 −26.401 1.00 36.83 C ATOM 4030 CB ILE 504 69.572 8.327 −24.978 1.00 36.83 C ATOM 4031 CG2 ILE 504 68.179 8.743 −24.487 1.00 36.83 C ATOM 4032 CG1 ILE 504 70.202 7.321 −24.014 1.00 36.83 C ATOM 4033 CD1 ILE 504 69.589 5.933 −24.071 1.00 36.83 C ATOM 4034 C ILE 504 68.877 8.754 −27.338 1.00 36.83 C ATOM 4035 O ILE 504 69.540 9.728 −27.692 1.00 36.83 O ATOM 4036 N ASP 505 67.630 8.530 −27.748 1.00 36.83 N ATOM 4037 CA ASP 505 66.917 9.465 −28.612 1.00 36.83 C ATOM 4038 CB ASP 505 65.892 8.726 −29.476 1.00 36.83 C ATOM 4039 CG ASP 505 65.456 9.532 −30.684 1.00 36.83 C ATOM 4040 OD1 ASP 505 65.283 10.770 −30.533 1.00 36.83 O ATOM 4041 OD2 ASP 505 65.278 8.928 −31.779 1.00 36.83 O ATOM 4042 C ASP 505 66.180 10.430 −27.680 1.00 36.83 C ATOM 4043 O ASP 505 65.117 10.107 −27.148 1.00 36.83 O ATOM 4044 N PHE 506 66.759 11.605 −27.461 1.00 36.83 N ATOM 4045 CA PHE 506 66.144 12.602 −26.591 1.00 36.83 C ATOM 4046 CB PHE 506 67.188 13.658 −26.197 1.00 36.83 C ATOM 4047 CG PHE 506 68.200 13.165 −25.194 1.00 36.83 C ATOM 4048 CD1 PHE 506 67.875 13.080 −23.839 1.00 36.83 C ATOM 4049 CD2 PHE 506 69.475 12.772 −25.599 1.00 36.83 C ATOM 4050 CE1 PHE 506 68.806 12.612 −22.902 1.00 36.83 C ATOM 4051 CE2 PHE 506 70.414 12.302 −24.669 1.00 36.83 C ATOM 4052 CZ PHE 506 70.079 12.223 −23.324 1.00 36.83 C ATOM 4053 C PHE 506 64.928 13.256 −27.268 1.00 36.83 C ATOM 4054 O PHE 506 64.223 14.065 −26.657 1.00 36.83 O ATOM 4055 N GLY 507 64.700 12.904 −28.533 1.00 36.83 N ATOM 4056 CA GLY 507 63.562 13.428 −29.279 1.00 36.83 C ATOM 4057 C GLY 507 63.471 14.915 −29.627 1.00 36.83 C ATOM 4058 O GLY 507 62.368 15.422 −29.849 1.00 36.83 O ATOM 4059 N LEU 508 64.599 15.621 −29.666 1.00 36.83 N ATOM 4060 CA LEU 508 64.592 17.051 −30.026 1.00 36.83 C ATOM 4061 CB LEU 508 65.377 17.902 −29.021 1.00 36.83 C ATOM 4062 CG LEU 508 65.006 17.928 −27.534 1.00 36.83 C ATOM 4063 CD1 LEU 508 63.538 18.293 −27.343 1.00 36.83 C ATOM 4064 CD2 LEU 508 65.308 16.583 −26.934 1.00 36.83 C ATOM 4065 C LEU 508 65.298 17.089 −31.364 1.00 36.83 C ATOM 4066 O LEU 508 66.484 16.746 −31.455 1.00 36.83 O ATOM 4067 N ASP 509 64.584 17.492 −32.408 1.00 36.83 N ATOM 4068 CA ASP 509 65.191 17.503 −33.731 1.00 36.83 C ATOM 4069 CB ASP 509 65.372 16.054 −34.209 1.00 36.83 C ATOM 4070 CG ASP 509 66.332 15.923 −35.381 1.00 36.83 C ATOM 4071 OD1 ASP 509 66.527 14.770 −35.831 1.00 36.83 O ATOM 4072 OD2 ASP 509 66.891 16.943 −35.855 1.00 36.83 O ATOM 4073 C ASP 509 64.287 18.268 −34.676 1.00 36.83 C ATOM 4074 O ASP 509 63.345 17.704 −35.252 1.00 36.83 O ATOM 4075 N SER 510 64.595 19.552 −34.843 1.00 36.83 N ATOM 4076 CA SER 510 63.815 20.427 −35.698 1.00 36.83 C ATOM 4077 CB SER 510 63.711 21.800 −35.048 1.00 36.83 C ATOM 4078 OG SER 510 64.981 22.398 −34.993 1.00 36.83 O ATOM 4079 C SER 510 64.402 20.569 −37.098 1.00 36.83 C ATOM 4080 O SER 510 64.240 21.613 −37.741 1.00 36.83 O ATOM 4081 N GLN 511 65.074 19.519 −37.570 1.00 36.83 N ATOM 4082 CA GLN 511 65.677 19.555 −38.899 1.00 36.83 C ATOM 4083 CB GLN 511 66.598 18.343 −39.111 1.00 36.83 C ATOM 4084 CG GLN 511 67.428 18.403 −40.402 1.00 36.83 C ATOM 4085 CD GLN 511 68.285 19.680 −40.531 1.00 36.83 C ATOM 4086 OE1 GLN 511 68.338 20.298 −41.601 1.00 36.83 O ATOM 4087 NE2 GLN 511 68.957 20.067 −39.451 1.00 36.83 N ATOM 4088 C GLN 511 64.595 19.594 −39.984 1.00 36.83 C ATOM 4089 O GLN 511 64.705 20.344 −40.954 1.00 36.83 O ATOM 4090 N ALA 512 63.547 18.798 −39.808 1.00 36.83 N ATOM 4091 CA ALA 512 62.467 18.759 −40.780 1.00 36.83 C ATOM 4092 CB ALA 512 61.413 17.761 −40.350 1.00 36.83 C ATOM 4093 C ALA 512 61.845 20.139 −40.959 1.00 36.83 C ATOM 4094 O ALA 512 61.524 20.534 −42.076 1.00 36.83 O ATOM 4095 N THR 513 61.676 20.878 −39.871 1.00 36.83 N ATOM 4096 CA THR 513 61.091 22.207 −39.979 1.00 36.83 C ATOM 4097 CB THR 513 60.756 22.796 −38.595 1.00 36.83 C ATOM 4098 OG1 THR 513 59.729 22.005 −37.990 1.00 36.83 O ATOM 4099 CG2 THR 513 60.284 24.252 −38.721 1.00 36.83 C ATOM 4100 C THR 513 62.062 23.119 −40.697 1.00 36.83 C ATOM 4101 O THR 513 61.669 23.908 −41.544 1.00 36.83 O ATOM 4102 N ILE 514 63.338 22.994 −40.358 1.00 36.83 N ATOM 4103 CA ILE 514 64.380 23.796 −40.983 1.00 36.83 C ATOM 4104 CB ILE 514 65.753 23.555 −40.279 1.00 36.83 C ATOM 4105 CG2 ILE 514 66.908 24.145 −41.119 1.00 36.83 C ATOM 4106 CG1 ILE 514 65.701 24.178 −38.876 1.00 36.83 C ATOM 4107 CD1 ILE 514 66.942 24.032 −38.065 1.00 36.83 C ATOM 4108 C ILE 514 64.470 23.493 −42.482 1.00 36.83 C ATOM 4109 O ILE 514 64.540 24.414 −43.303 1.00 36.83 O ATOM 4110 N ASP 515 64.462 22.208 −42.839 1.00 36.83 N ATOM 4111 CA ASP 515 64.520 21.819 −44.247 1.00 36.83 C ATOM 4112 CB ASP 515 64.587 20.284 −44.399 1.00 36.83 C ATOM 4113 CG ASP 515 65.889 19.668 −43.837 1.00 36.83 C ATOM 4114 OD1 ASP 515 65.953 18.423 −43.731 1.00 36.83 O ATOM 4115 OD2 ASP 515 66.847 20.406 −43.502 1.00 36.83 O ATOM 4116 C ASP 515 63.265 22.358 −44.971 1.00 36.83 C ATOM 4117 O ASP 515 63.333 22.734 −46.129 1.00 36.83 O ATOM 4118 N LEU 516 62.122 22.412 −44.294 1.00 36.83 N ATOM 4119 CA LEU 516 60.912 22.925 −44.944 1.00 36.83 C ATOM 4120 CB LEU 516 59.683 22.770 −44.046 1.00 36.83 C ATOM 4121 CG LEU 516 58.429 23.554 −44.474 1.00 36.83 C ATOM 4122 CD1 LEU 516 57.937 23.085 −45.838 1.00 36.83 C ATOM 4123 CD2 LEU 516 57.350 23.378 −43.446 1.00 36.83 C ATOM 4124 C LEU 516 61.037 24.389 −45.342 1.00 36.83 C ATOM 4125 O LEU 516 60.424 24.830 −46.300 1.00 36.83 O ATOM 4126 N ILE 517 61.839 25.142 −44.609 1.00 36.83 N ATOM 4127 CA ILE 517 61.998 26.547 −44.913 1.00 36.83 C ATOM 4128 CB ILE 517 62.180 27.380 −43.605 1.00 36.83 C ATOM 4129 CG2 ILE 517 62.380 28.872 −43.941 1.00 36.83 C ATOM 4130 CG1 ILE 517 60.954 27.206 −42.706 1.00 36.83 C ATOM 4131 CD1 ILE 517 61.140 27.752 −41.314 1.00 36.83 C ATOM 4132 C ILE 517 63.152 26.848 −45.870 1.00 36.83 C ATOM 4133 O ILE 517 62.945 27.482 −46.902 1.00 36.83 O ATOM 4134 N ASP 518 64.357 26.389 −45.537 1.00 36.83 N ATOM 4135 CA ASP 518 65.514 26.683 −46.369 1.00 36.83 C ATOM 4136 CB ASP 518 66.667 27.202 −45.496 1.00 36.83 C ATOM 4137 CG ASP 518 67.335 26.108 −44.666 1.00 36.83 C ATOM 4138 OD1 ASP 518 68.181 26.452 −43.811 1.00 36.83 O ATOM 4139 OD2 ASP 518 67.029 24.918 −44.854 1.00 36.83 O ATOM 4140 C ASP 518 66.039 25.601 −47.307 1.00 36.83 C ATOM 4141 O ASP 518 67.003 25.840 −48.012 1.00 36.83 O ATOM 4142 N GLY 519 65.416 24.427 −47.328 1.00 36.83 N ATOM 4143 CA GLY 519 65.879 23.368 −48.211 1.00 36.83 C ATOM 4144 C GLY 519 66.050 23.791 −49.662 1.00 36.83 C ATOM 4145 O GLY 519 65.244 24.545 −50.198 1.00 36.83 O ATOM 4146 N ARG 520 67.107 23.328 −50.315 1.00 36.83 N ATOM 4147 CA ARG 520 67.295 23.693 −51.710 1.00 36.83 C ATOM 4148 CB ARG 520 68.778 23.959 −52.007 1.00 36.83 C ATOM 4149 CG ARG 520 69.035 24.606 −53.371 1.00 36.83 C ATOM 4150 CD ARG 520 70.511 25.016 −53.558 1.00 36.83 C ATOM 4151 NE ARG 520 71.409 23.931 −53.167 1.00 36.83 N ATOM 4152 CZ ARG 520 71.635 22.837 −53.886 1.00 36.83 C ATOM 4153 NH1 ARG 520 71.038 22.675 −55.063 1.00 36.83 N ATOM 4154 NH2 ARG 520 72.434 21.887 −53.405 1.00 36.83 N ATOM 4155 C ARG 520 66.726 22.597 −52.611 1.00 36.83 C ATOM 4156 O ARG 520 65.926 22.880 −53.503 1.00 36.83 O ATOM 4157 N GLN 521 67.104 21.345 −52.373 1.00 36.83 N ATOM 4158 CA GLN 521 66.588 20.238 −53.180 1.00 36.83 C ATOM 4159 CB GLN 521 67.626 19.806 −54.228 1.00 36.83 C ATOM 4160 CG GLN 521 69.042 19.590 −53.671 1.00 36.83 C ATOM 4161 CD GLN 521 70.053 19.222 −54.754 1.00 36.83 C ATOM 4162 OE1 GLN 521 70.365 18.034 −54.979 1.00 36.83 O ATOM 4163 NE2 GLN 521 70.566 20.246 −55.444 1.00 36.83 N ATOM 4164 C GLN 521 66.216 19.038 −52.310 1.00 36.83 C ATOM 4165 O GLN 521 67.086 18.437 −51.679 1.00 36.83 O ATOM 4166 N PRO 522 64.913 18.693 −52.235 1.00 36.83 N ATOM 4167 CD PRO 522 64.405 17.640 −51.337 1.00 36.83 C ATOM 4168 CA PRO 522 63.809 19.364 −52.925 1.00 36.83 C ATOM 4169 CB PRO 522 62.613 18.479 −52.597 1.00 36.83 C ATOM 4170 CG PRO 522 62.939 17.983 −51.218 1.00 36.83 C ATOM 4171 C PRO 522 63.662 20.783 −52.382 1.00 36.83 C ATOM 4172 O PRO 522 64.021 21.049 −51.237 1.00 36.83 O ATOM 4173 N PRO 523 63.131 21.708 −53.198 1.00 36.83 N ATOM 4174 CD PRO 523 62.677 21.507 −54.585 1.00 36.83 C ATOM 4175 CA PRO 523 62.950 23.107 −52.785 1.00 36.83 C ATOM 4176 CB PRO 523 62.500 23.788 −54.073 1.00 36.83 C ATOM 4177 CG PRO 523 61.784 22.698 −54.795 1.00 36.83 C ATOM 4178 C PRO 523 62.020 23.416 −51.609 1.00 36.83 C ATOM 4179 O PRO 523 60.856 23.043 −51.606 1.00 36.83 O ATOM 4180 N GLY 524 62.549 24.100 −50.605 1.00 36.83 N ATOM 4181 CA GLY 524 61.728 24.493 −49.470 1.00 36.83 C ATOM 4182 C GLY 524 60.944 25.770 −49.800 1.00 36.83 C ATOM 4183 O GLY 524 60.937 26.232 −50.939 1.00 36.83 O ATOM 4184 N ILE 525 60.290 26.352 −48.801 1.00 36.83 N ATOM 4185 CA ILE 525 59.504 27.563 −48.991 1.00 36.83 C ATOM 4186 CB ILE 525 58.842 27.985 −47.658 1.00 36.83 C ATOM 4187 CG2 ILE 525 58.045 29.289 −47.833 1.00 36.83 C ATOM 4188 CG1 ILE 525 57.941 26.849 −47.160 1.00 36.83 C ATOM 4189 CD1 ILE 525 57.292 27.107 −45.816 1.00 36.83 C ATOM 4190 C ILE 525 60.318 28.733 −49.554 1.00 36.83 C ATOM 4191 O ILE 525 59.950 29.304 −50.591 1.00 36.83 O ATOM 4192 N LEU 526 61.420 29.090 −48.891 1.00 36.83 N ATOM 4193 CA LEU 526 62.242 30.204 −49.353 1.00 36.83 C ATOM 4194 CB LEU 526 63.423 30.439 −48.403 1.00 36.83 C ATOM 4195 CG LEU 526 63.118 30.892 −46.966 1.00 36.83 C ATOM 4196 CD1 LEU 526 64.420 31.221 −46.258 1.00 36.83 C ATOM 4197 CD2 LEU 526 62.214 32.091 −46.977 1.00 36.83 C ATOM 4198 C LEU 526 62.747 30.034 −50.789 1.00 36.83 C ATOM 4199 O LEU 526 62.922 31.017 −51.499 1.00 36.83 O ATOM 4200 N ALA 527 62.971 28.792 −51.217 1.00 36.83 N ATOM 4201 CA ALA 527 63.425 28.521 −52.584 1.00 36.83 C ATOM 4202 CB ALA 527 63.879 27.081 −52.721 1.00 36.83 C ATOM 4203 C ALA 527 62.272 28.797 −53.545 1.00 36.83 C ATOM 4204 O ALA 527 62.434 29.483 −54.560 1.00 36.83 O ATOM 4205 N LEU 528 61.098 28.273 −53.210 1.00 36.83 N ATOM 4206 CA LEU 528 59.924 28.484 −54.050 1.00 36.83 C ATOM 4207 CB LEU 528 58.749 27.634 −53.535 1.00 36.83 C ATOM 4208 CG LEU 528 58.961 26.116 −53.673 1.00 36.83 C ATOM 4209 CD1 LEU 528 57.831 25.359 −53.022 1.00 36.83 C ATOM 4210 CD2 LEU 528 59.073 25.742 −55.157 1.00 36.83 C ATOM 4211 C LEU 528 59.561 29.977 −54.106 1.00 36.83 C ATOM 4212 O LEU 528 59.130 30.479 −55.146 1.00 36.83 O ATOM 4213 N LEU 529 59.753 30.691 −52.998 1.00 36.83 N ATOM 4214 CA LEU 529 59.456 32.119 −52.971 1.00 36.83 C ATOM 4215 CB LEU 529 59.638 32.692 −51.558 1.00 36.83 C ATOM 4216 CG LEU 529 59.721 34.230 −51.445 1.00 36.83 C ATOM 4217 CD1 LEU 529 58.376 34.877 −51.745 1.00 36.83 C ATOM 4218 CD2 LEU 529 60.177 34.610 −50.051 1.00 36.83 C ATOM 4219 C LEU 529 60.377 32.858 −53.936 1.00 36.83 C ATOM 4220 O LEU 529 59.932 33.754 −54.655 1.00 36.83 O ATOM 4221 N ASP 530 61.661 32.488 −53.946 1.00 36.83 N ATOM 4222 CA ASP 530 62.640 33.133 −54.825 1.00 36.83 C ATOM 4223 CB ASP 530 64.059 32.630 −54.529 1.00 36.83 C ATOM 4224 CG ASP 530 64.659 33.262 −53.286 1.00 36.83 C ATOM 4225 OD1 ASP 530 63.983 34.102 −52.646 1.00 36.83 O ATOM 4226 OD2 ASP 530 65.816 32.922 −52.952 1.00 36.83 O ATOM 4227 C ASP 530 62.312 32.878 −56.289 1.00 36.83 C ATOM 4228 O ASP 530 62.344 33.793 −57.108 1.00 36.83 O ATOM 4229 N GLU 531 62.006 31.622 −56.601 1.00 36.83 N ATOM 4230 CA GLU 531 61.657 31.230 −57.958 1.00 36.83 C ATOM 4231 CB GLU 531 61.297 29.750 −57.973 1.00 36.83 C ATOM 4232 CG GLU 531 60.848 29.219 −59.308 1.00 36.83 C ATOM 4233 CD GLU 531 60.413 27.764 −59.208 1.00 36.83 C ATOM 4234 OE1 GLU 531 61.269 26.893 −58.904 1.00 36.83 O ATOM 4235 OE2 GLU 531 59.212 27.495 −59.421 1.00 36.83 O ATOM 4236 C GLU 531 60.480 32.080 −58.439 1.00 36.83 C ATOM 4237 O GLU 531 60.484 32.588 −59.552 1.00 36.83 O ATOM 4238 N GLN 532 59.481 32.249 −57.584 1.00 36.83 N ATOM 4239 CA GLN 532 58.326 33.053 −57.942 1.00 36.83 C ATOM 4240 CB GLN 532 57.229 32.890 −56.895 1.00 36.83 C ATOM 4241 CG GLN 532 56.484 31.568 −56.963 1.00 36.83 C ATOM 4242 CD GLN 532 55.302 31.632 −57.907 1.00 36.83 C ATOM 4243 OE1 GLN 532 54.374 32.415 −57.700 1.00 36.83 O ATOM 4244 NE2 GLN 532 55.330 30.817 −58.952 1.00 36.83 N ATOM 4245 C GLN 532 58.745 34.518 −58.044 1.00 36.83 C ATOM 4246 O GLN 532 58.211 35.274 −58.857 1.00 36.83 O ATOM 4247 N SER 533 59.705 34.917 −57.220 1.00 36.83 N ATOM 4248 CA SER 533 60.176 36.298 −57.227 1.00 36.83 C ATOM 4249 CB SER 533 61.230 36.519 −56.141 1.00 36.83 C ATOM 4250 OG SER 533 60.620 36.803 −54.898 1.00 36.83 O ATOM 4251 C SER 533 60.749 36.711 −58.571 1.00 36.83 C ATOM 4252 O SER 533 60.685 37.878 −58.939 1.00 36.83 O ATOM 4253 N VAL 534 61.299 35.747 −59.300 1.00 36.83 N ATOM 4254 CA VAL 534 61.891 36.009 −60.603 1.00 36.83 C ATOM 4255 CB VAL 534 63.165 35.157 −60.814 1.00 36.83 C ATOM 4256 CG1 VAL 534 64.219 35.512 −59.784 1.00 36.83 C ATOM 4257 CG2 VAL 534 62.823 33.695 −60.716 1.00 36.83 C ATOM 4258 C VAL 534 60.933 35.729 −61.763 1.00 36.83 C ATOM 4259 O VAL 534 61.270 36.004 −62.914 1.00 36.83 O ATOM 4260 N PHE 535 59.763 35.163 −61.472 1.00 36.83 N ATOM 4261 CA PHE 535 58.776 34.874 −62.509 1.00 36.83 C ATOM 4262 CB PHE 535 57.860 33.721 −62.096 1.00 36.83 C ATOM 4263 CG PHE 535 56.862 33.338 −63.150 1.00 36.83 C ATOM 4264 CD1 PHE 535 57.283 32.870 −64.385 1.00 36.83 C ATOM 4265 CD2 PRE 535 55.496 33.467 −62.920 1.00 36.83 C ATOM 4266 CE1 PHE 535 56.367 32.540 −65.368 1.00 36.83 C ATOM 4267 CE2 PHE 535 54.564 33.137 −63.911 1.00 36.83 C ATOM 4268 CZ PHE 535 55.003 32.675 −65.129 1.00 36.83 C ATOM 4269 C PHE 535 57.955 36.141 −62.725 1.00 36.83 C ATOM 4270 O PHE 535 57.207 36.570 −61.850 1.00 36.83 O ATOM 4271 N PRO 536 58.086 36.753 −63.915 1.00 36.83 N ATOM 4272 CD PRO 536 58.798 36.146 −65.058 1.00 36.83 C ATOM 4273 CA PRO 536 57.403 37.991 −64.329 1.00 36.83 C ATOM 4274 CB PRO 536 57.615 38.016 −65.849 1.00 36.83 C ATOM 4275 CG PRO 536 58.914 37.315 −66.020 1.00 36.83 C ATOM 4276 C PRO 536 55.931 38.137 −63.954 1.00 36.83 C ATOM 4277 O PRO 536 55.548 39.126 −63.345 1.00 36.83 O ATOM 4278 N ASN 537 55.120 37.151 −64.319 1.00 36.83 N ATOM 4279 CA ASN 537 53.680 37.151 −64.070 1.00 36.83 C ATOM 4280 CB ASN 537 52.992 36.320 −65.165 1.00 36.83 C ATOM 4281 CG ASN 537 53.451 36.711 −66.574 1.00 36.83 C ATOM 4282 OD1 ASN 537 53.508 37.894 −66.905 1.00 36.83 O ATOM 4283 ND2 ASN 537 53.773 35.716 −67.405 1.00 36.83 N ATOM 4284 C ASN 537 53.252 36.616 −62.701 1.00 36.83 C ATOM 4285 O ASN 537 52.069 36.342 −62.481 1.00 36.83 O ATOM 4286 N ALA 538 54.193 36.468 −61.776 1.00 36.83 N ATOM 4287 CA ALA 538 53.856 35.938 −60.459 1.00 36.83 C ATOM 4288 CB ALA 538 55.126 35.625 −59.668 1.00 36.83 C ATOM 4289 C ALA 538 52.968 36.857 −59.648 1.00 36.83 C ATOM 4290 O ALA 538 53.003 38.070 −59.810 1.00 36.83 O ATOM 4291 N THR 539 52.161 36.251 −58.780 1.00 36.83 N ATOM 4292 CA THR 539 51.267 36.981 −57.882 1.00 36.83 C ATOM 4293 CB THR 539 49.812 36.938 −58.356 1.00 36.83 C ATOM 4294 OG1 THR 539 49.405 35.573 −58.466 1.00 36.83 O ATOM 4295 CG2 THR 539 49.648 37.645 −59.690 1.00 36.83 C ATOM 4296 C TER 539 51.304 36.299 −56.508 1.00 36.83 C ATOM 4297 O THR 539 51.795 35.180 −56.382 1.00 36.83 O ATOM 4298 N ASP 540 50.782 36.966 −55.485 1.00 36.83 N ATOM 4299 CA ASP 540 50.753 36.368 −54.165 1.00 36.83 C ATOM 4300 CB ASP 540 50.212 37.359 −53.128 1.00 36.83 C ATOM 4301 CG ASP 540 51.192 38.489 −52.823 1.00 36.83 C ATOM 4302 OD1 ASP 540 52.404 38.351 −53.130 1.00 36.83 O ATOM 4303 OD2 ASP 540 50.743 39.519 −52.265 1.00 36.83 O ATOM 4304 C ASP 540 49.869 35.128 −54.209 1.00 36.83 C ATOM 4305 O ASP 540 50.080 34.180 −53.457 1.00 36.83 O ATOM 4306 N ASN 541 48.894 35.135 −55.115 1.00 36.83 N ATOM 4307 CA ASN 541 47.965 34.017 −55.279 1.00 36.83 C ATOM 4308 CB ASN 541 46.764 34.448 −56.144 1.00 36.83 C ATOM 4309 CG ASN 541 46.118 35.772 −55.661 1.00 36.83 C ATOM 4310 OD1 ASN 541 45.306 35.787 −54.734 1.00 36.83 O ATOM 4311 ND2 ASN 541 46.497 36.885 −56.296 1.00 36.83 N ATOM 4312 C ASN 541 48.690 32.823 −55.922 1.00 36.83 C ATOM 4313 O ASN 541 48.491 31.679 −55.509 1.00 36.83 O ATOM 4314 N THR 542 49.533 33.075 −56.923 1.00 36.83 N ATOM 4315 CA THR 542 50.274 31.970 −57.553 1.00 36.83 C ATOM 4316 CB THR 542 51.000 32.392 −58.855 1.00 36.83 C ATOM 4317 OG1 THR 542 51.889 33.476 −58.573 1.00 36.83 O ATOM 4318 CG2 THR 542 49.997 32.812 −59.927 1.00 36.83 C ATOM 4319 C THR 542 51.332 31.438 −56.586 1.00 36.83 C ATOM 4320 O THR 542 51.645 30.254 −56.593 1.00 36.83 O ATOM 4321 N LEU 543 51.894 32.315 −55.759 1.00 36.83 N ATOM 4322 CA LEU 543 52.891 31.874 −54.793 1.00 36.83 C ATOM 4323 CB LEU 543 53.546 33.077 −54.109 1.00 36.83 C ATOM 4324 CG LEU 543 54.352 32.772 −52.843 1.00 36.83 C ATOM 4325 CD1 LEU 543 55.529 31.877 −53.155 1.00 36.83 C ATOM 4326 CD2 LEU 543 54.822 34.088 −52.245 1.00 36.83 C ATOM 4327 C LEU 543 52.320 30.908 −53.727 1.00 36.83 C ATOM 4328 O LEU 543 52.924 29.863 −53.466 1.00 36.83 O ATOM 4329 N ILE 544 51.173 31.241 −53.130 1.00 36.83 N ATOM 4330 CA ILE 544 50.567 30.383 −52.108 1.00 36.83 C ATOM 4331 CB ILE 544 49.315 31.064 −51.434 1.00 36.83 C ATOM 4332 CG2 ILE 544 48.186 31.237 −52.444 1.00 36.83 C ATOM 4333 CG1 ILE 544 48.784 30.222 −50.269 1.00 36.83 C ATOM 4334 CD1 ILE 544 49.612 30.264 −49.038 1.00 36.83 C ATOM 4335 C ILE 544 50.164 29.060 −52.751 1.00 36.83 C ATOM 4336 O ILE 544 50.324 27.993 −52.150 1.00 36.83 O ATOM 4337 N THR 545 49.662 29.129 −53.980 1.00 36.83 N ATOM 4338 CA THR 545 49.247 27.933 −54.705 1.00 36.83 C ATOM 4339 CB THR 545 48.558 28.294 −56.054 1.00 36.83 C ATOM 4340 OG1 THR 545 47.459 29.174 −55.809 1.00 36.83 O ATOM 4341 CG2 TER 545 48.030 27.058 −56.741 1.00 36.83 C ATOM 4342 C THR 545 50.466 27.054 −54.964 1.00 36.83 C ATOM 4343 O THR 545 50.390 25.833 −54.895 1.00 36.83 O ATOM 4344 N LYS 546 51.598 27.679 −55.254 1.00 36.83 N ATOM 4345 CA LYS 546 52.815 26.919 −55.488 1.00 36.83 C ATOM 4346 CB LYS 546 53.937 27.838 −55.973 1.00 36.83 C ATOM 4347 CG LYS 546 55.241 27.118 −56.287 1.00 36.83 C ATOM 4348 CD LYS 546 55.107 26.221 −57.509 1.00 36.83 C ATOM 4349 CE LYS 546 56.454 25.630 −57.929 1.00 36.83 C ATOM 4350 NZ LYS 546 56.311 24.541 −58.960 1.00 36.83 N ATOM 4351 C LYS 546 53.219 26.244 −54.186 1.00 36.83 C ATOM 4352 O LYS 546 53.589 25.072 −54.177 1.00 36.83 O ATOM 4353 N LEU 547 53.141 26.983 −53.084 1.00 36.83 N ATOM 4354 CA LEU 547 53.502 26.431 −51.782 1.00 36.83 C ATOM 4355 CB LEU 547 53.449 27.513 −50.696 1.00 36.83 C ATOM 4356 CG LEU 547 54.416 28.695 −50.820 1.00 36.83 C ATOM 4357 CD1 LEU 547 54.166 29.677 −49.686 1.00 36.83 C ATOM 4358 CD2 LEU 547 55.862 28.204 −50.780 1.00 36.83 C ATOM 4359 C LEU 547 52.601 25.255 −51.404 1.00 36.83 C ATOM 4360 O LEU 547 53.096 24.208 −50.992 1.00 36.83 O ATOM 4361 N HIS 548 51.284 25.413 −51.539 1.00 36.83 N ATOM 4362 CA HIS 548 50.373 24.306 −51.220 1.00 36.83 C ATOM 4363 CB HIS 548 48.903 24.705 −51.397 1.00 36.83 C ATOM 4364 CG HIS 548 48.423 25.723 −50.414 1.00 36.83 C ATOM 4365 CD2 HIS 548 47.567 26.759 −50.555 1.00 36.83 C ATOM 4366 ND1 HIS 548 48.812 25.723 −49.093 1.00 36.83 N ATOM 4367 CE1 HIS 548 48.217 26.719 −48.462 1.00 36.83 C ATOM 4368 NE2 HIS 548 47.455 27.363 −49.326 1.00 36.83 N ATOM 4369 C HIS 548 50.634 23.110 −52.130 1.00 36.83 C ATOM 4370 O HIS 548 50.587 21.954 −51.699 1.00 36.83 O ATOM 4371 N SER 549 50.911 23.388 −53.392 1.00 36.83 N ATOM 4372 CA SER 549 51.136 22.308 −54.333 1.00 36.83 C ATOM 4373 CB SER 549 51.355 22.865 −55.735 1.00 36.83 C ATOM 4374 OG SER 549 51.425 21.807 −56.670 1.00 36.83 O ATOM 4375 C SER 549 52.316 21.430 −53.926 1.00 36.83 C ATOM 4376 O SER 549 52.284 20.215 −54.105 1.00 36.83 O ATOM 4377 N HIS 550 53.351 22.038 −53.362 1.00 36.83 N ATOM 4378 CA HIS 550 54.511 21.270 −52.953 1.00 36.83 C ATOM 4379 CB HIS 550 55.766 22.140 −52.973 1.00 36.83 C ATOM 4380 CG HIS 550 56.292 22.424 −54.347 1.00 36.83 C ATOM 4381 CD2 HIS 550 55.733 23.064 −55.401 1.00 36.83 C ATOM 4382 ND1 HIS 550 57.575 22.100 −54.732 1.00 36.83 N ATOM 4383 CE1 HIS 550 57.785 22.334 −55.961 1.00 36.83 C ATOM 4384 NE2 HIS 550 56.682 23.123 −56.388 1.00 36.83 N ATOM 4385 C HIS 550 54.418 20.608 −51.587 1.00 36.83 C ATOM 4386 O HIS 550 54.818 19.458 −51.432 1.00 36.83 O ATOM 4387 N PHE 551 53.855 21.310 −50.608 1.00 36.83 N ATOM 4388 CA PHE 551 53.823 20.787 −49.247 1.00 36.83 C ATOM 4389 CB PHE 551 54.489 21.816 −48.326 1.00 36.83 C ATOM 4390 CG PINE 551 55.773 22.361 −48.879 1.00 36.83 C ATOM 4391 CD1 PHE 551 56.855 21.517 −49.116 1.00 36.83 C ATOM 4392 CD2 PHE 551 55.890 23.712 −49.200 1.00 36.83 C ATOM 4393 CE1 PHE 551 58.027 22.008 −49.666 1.00 36.83 C ATOM 4394 CE2 PHE 551 57.060 24.220 −49.752 1.00 36.83 C ATOM 4395 CZ PHE 551 58.133 23.373 −49.989 1.00 36.83 C ATOM 4396 C PHE 551 52.520 20.311 −48.618 1.00 36.83 C ATOM 4397 O PHE 551 52.551 19.567 −47.645 1.00 36.83 O ATOM 4398 N SER 552 51.378 20.711 −49.152 1.00 36.83 N ATOM 4399 CA SER 552 50.124 20.280 −48.550 1.00 36.83 C ATOM 4400 CB SER 552 48.955 20.917 −49.274 1.00 36.83 C ATOM 4401 OG SER 552 47.766 20.579 −48.605 1.00 36.83 O ATOM 4402 C SER 552 49.951 18.757 −48.530 1.00 36.83 C ATOM 4403 O SER 552 50.056 18.093 −49.559 1.00 36.83 O ATOM 4404 N LYS 553 49.671 18.213 −47.352 1.00 36.83 N ATOM 4405 CA LYS 553 49.489 16.768 −47.198 1.00 36.83 C ATOM 4406 CB LYS 553 48.267 16.283 −47.991 1.00 36.83 C ATOM 4407 CG LYS 553 46.945 16.820 −47.458 1.00 36.83 C ATOM 4408 CD LYS 553 45.769 16.199 −48.174 1.00 36.83 C ATOM 4409 CE LYS 553 44.582 17.158 −48.235 1.00 36.83 C ATOM 4410 NZ LYS 553 44.897 18.311 −49.139 1.00 36.83 N ATOM 4411 C LYS 553 50.725 15.982 −47.629 1.00 36.83 C ATOM 4412 O LYS 553 50.631 14.823 −48.033 1.00 36.83 O ATOM 4413 N LYS 554 51.887 16.619 −47.545 1.00 36.83 N ATOM 4414 CA LYS 554 53.124 15.953 −47.911 1.00 36.83 C ATOM 4415 CB LYS 554 53.602 16.447 −49.274 1.00 36.83 C ATOM 4416 CG LYS 554 52.607 16.193 −50.377 1.00 36.83 C ATOM 4417 CD LYS 554 53.246 16.382 −51.731 1.00 36.83 C ATOM 4418 CE LYS 554 52.215 16.658 −52.789 1.00 36.83 C ATOM 4419 NZ LYS 554 52.868 17.238 −53.991 1.00 36.83 N ATOM 4420 C LYS 554 54.186 16.180 −46.843 1.00 36.83 C ATOM 4421 O LYS 554 54.854 15.250 −46.411 1.00 36.83 O ATOM 4422 N ASN 555 54.335 17.420 −46.400 1.00 36.83 N ATOM 4423 CA ASN 555 55.308 17.708 −45.363 1.00 36.83 C ATOM 4424 CB ASN 555 56.021 19.028 −45.646 1.00 36.83 C ATOM 4425 CG ASN 555 57.250 19.211 −44.791 1.00 36.83 C ATOM 4426 OD1 ASN 555 58.352 19.414 −45.302 1.00 36.83 O ATOM 4427 ND2 ASN 555 57.074 19.137 −43.478 1.00 36.83 N ATOM 4428 C ASN 555 54.564 17.771 −44.036 1.00 36.83 C ATOM 4429 O ASN 555 53.637 18.557 −43.869 1.00 36.83 O ATOM 4430 N ALA 556 54.983 16.931 −43.098 1.00 36.83 N ATOM 4431 CA ALA 556 54.376 16.855 −41.781 1.00 36.83 C ATOM 4432 CB ALA 556 54.961 15.662 −41.010 1.00 36.83 C ATOM 4433 C ALA 556 54.518 18.129 −40.950 1.00 36.83 C ATOM 4434 O ALA 556 53.936 18.227 −39.884 1.00 36.83 O ATOM 4435 N LYS 557 55.293 19.100 −41.417 1.00 36.83 N ATOM 4436 CA LYS 557 55.436 20.340 −40.662 1.00 36.83 C ATOM 4437 CB LYS 557 56.916 20.715 −40.521 1.00 36.83 C ATOM 4438 CG LYS 557 57.781 19.689 −39.821 1.00 36.83 C ATOM 4439 CD LYS 557 57.314 19.428 −38.407 1.00 36.83 C ATOM 4440 CE LYS 557 58.224 18.436 −37.709 1.00 36.83 C ATOM 4441 NZ LYS 557 57.904 18.315 −36.266 1.00 36.83 N ATOM 4442 C LYS 557 54.678 21.486 −41.350 1.00 36.83 C ATOM 4443 O LYS 557 54.693 22.631 −40.888 1.00 36.83 O ATOM 4444 N TYR 558 54.014 21.163 −42.456 1.00 36.83 N ATOM 4445 CA TYR 558 53.268 22.148 −43.220 1.00 36.83 C ATOM 4446 CB TYR 558 53.731 22.110 −44.671 1.00 36.83 C ATOM 4447 CG TYR 558 53.128 23.177 −45.557 1.00 36.83 C ATOM 4448 CD1 TYR 558 51.876 23.005 −46.139 1.00 36.83 C ATOM 4449 CE1 TYR 558 51.337 23.968 −46.992 1.00 36.83 C ATOM 4450 CD2 TYR 558 53.826 24.345 −45.839 1.00 36.83 C ATOM 4451 CE2 TYR 558 53.297 25.312 −46.680 1.00 36.83 C ATOM 4452 CZ TYR 558 52.052 25.118 −47.265 1.00 36.83 C ATOM 4453 OH TYR 558 51.553 26.040 −48.167 1.00 36.83 O ATOM 4454 C TYR 558 51.761 21.946 −43.144 1.00 36.83 C ATOM 4455 O TYR 558 51.264 20.833 −43.005 1.00 36.83 O ATOM 4456 N GLU 559 51.018 23.034 −43.238 1.00 36.83 N ATOM 4457 CA GLU 559 49.584 22.907 −43.170 1.00 36.83 C ATOM 4458 CB GLU 559 49.107 23.104 −41.726 1.00 36.83 C ATOM 4459 CG GLU 559 47.611 22.848 −41.503 1.00 36.83 C ATOM 4460 CD GLU 559 47.229 22.845 −40.021 1.00 36.83 C ATOM 4461 OE1 GLU 559 47.714 21.984 −39.253 1.00 36.83 O ATOM 4462 OE2 GLU 559 46.442 23.708 −39.606 1.00 36.83 O ATOM 4463 C GLU 559 48.863 23.873 −44.083 1.00 36.83 C ATOM 4464 O GLU 559 49.049 25.087 −44.004 1.00 36.83 O ATOM 4465 N GLU 560 48.069 23.321 −44.986 1.00 36.83 N ATOM 4466 CA GLU 560 47.252 24.147 −45.847 1.00 36.83 C ATOM 4467 CB GLU 560 46.931 23.468 −47.160 1.00 36.83 C ATOM 4468 CG GLU 560 46.010 24.320 −48.013 1.00 36.83 C ATOM 4469 CD GLU 560 45.669 23.673 −49.336 1.00 36.83 C ATOM 4470 OE1 GLU 560 46.528 22.961 −49.888 1.00 36.83 O ATOM 4471 OE2 GLU 560 44.550 23.894 −49.831 1.00 36.83 O ATOM 4472 C GLU 560 45.969 24.285 −45.048 1.00 36.83 C ATOM 4473 O GLU 560 45.256 23.311 −44.837 1.00 36.83 O ATOM 4474 N PRO 561 45.666 25.495 −44.578 1.00 36.83 N ATOM 4475 CD PRO 561 46.419 26.745 −44.771 1.00 36.83 C ATOM 4476 CA PRO 561 44.445 25.708 −43.792 1.00 36.83 C ATOM 4477 CB PRO 561 44.671 27.090 −43.187 1.00 36.83 C ATOM 4478 CG PRO 561 45.457 27.793 −44.278 1.00 36.83 C ATOM 4479 C PRO 561 43.153 25.638 −44.606 1.00 36.83 C ATOM 4480 O PRO 561 43.125 26.023 −45.781 1.00 36.83 O ATOM 4481 N ARG 562 42.092 25.148 −43.968 1.00 36.83 N ATOM 4482 CA ARG 562 40.780 25.036 −44.593 1.00 36.83 C ATOM 4483 CB ARG 562 39.970 23.903 −43.939 1.00 36.83 C ATOM 4484 CG ARG 562 40.422 22.486 −44.292 1.00 36.83 C ATOM 4485 CD ARG 562 39.464 21.471 −43.708 1.00 36.83 C ATOM 4486 NE ARG 562 39.593 21.399 −42.263 1.00 36.83 N ATOM 4487 CZ ARG 562 38.610 21.097 −41.423 1.00 36.83 C ATOM 4488 NH1 ARG 562 37.390 20.839 −41.880 1.00 36.83 N ATOM 4489 NH2 ARG 562 38.861 21.021 −40.122 1.00 36.83 N ATOM 4490 C ARG 562 39.991 26.340 −44.458 1.00 36.83 C ATOM 4491 O ARG 562 39.024 26.586 −45.184 1.00 36.83 O ATOM 4492 N PHE 563 40.421 27.175 −43.524 1.00 36.83 N ATOM 4493 CA PHE 563 39.748 28.429 −43.246 1.00 36.83 C ATOM 4494 CB PHE 563 39.751 28.650 −41.734 1.00 36.83 C ATOM 4495 CG PHE 563 41.130 28.756 −41.149 1.00 36.83 C ATOM 4496 CD1 PHE 563 41.865 29.932 −41.278 1.00 36.83 C ATOM 4497 CD2 PHE 563 41.715 27.660 −40.520 1.00 36.83 C ATOM 4498 CE1 PHE 563 43.161 30.013 −40.795 1.00 36.83 C ATOM 4499 CE2 PHE 563 43.009 27.732 −40.034 1.00 36.83 C ATOM 4500 CZ PHE 563 43.738 28.913 −40.173 1.00 36.83 C ATOM 4501 C PHE 563 40.321 29.658 −43.956 1.00 36.83 C ATOM 4502 O PHE 563 39.829 30.767 −43.755 1.00 36.83 O ATOM 4503 N SER 564 41.351 29.472 −44.774 1.00 36.83 N ATOM 4504 CA SER 564 41.954 30.584 −45.495 1.00 36.83 C ATOM 4505 CB SER 564 42.957 31.324 −44.604 1.00 36.83 C ATOM 4506 OG SER 564 43.601 32.350 −45.338 1.00 36.83 O ATOM 4507 C SER 564 42.663 30.131 −46.765 1.00 36.83 C ATOM 4508 O SER 564 43.188 29.030 −46.826 1.00 36.83 O ATOM 4509 N LYS 565 42.680 30.998 −47.770 1.00 36.83 N ATOM 4510 CA LYS 565 43.329 30.712 −49.048 1.00 36.83 C ATOM 4511 CB LYS 565 42.370 31.017 −50.195 1.00 36.83 C ATOM 4512 CG LYS 565 41.137 30.143 −50.207 1.00 36.83 C ATOM 4513 CD LYS 565 40.201 30.612 −51.282 1.00 36.83 C ATOM 4514 CE LYS 565 38.796 30.055 −51.079 1.00 36.83 C ATOM 4515 NZ LYS 565 37.853 30.683 −52.053 1.00 36.83 N ATOM 4516 C LYS 565 44.597 31.542 −49.223 1.00 36.83 C ATOM 4517 O LYS 565 45.284 31.441 −50.230 1.00 36.83 O ATOM 4518 N THR 566 44.896 32.363 −48.225 1.00 36.83 N ATOM 4519 CA THR 566 46.067 33.222 −48.262 1.00 36.83 C ATOM 4520 CB THR 566 45.658 34.733 −48.207 1.00 36.83 C ATOM 4521 OG1 THR 566 45.026 35.032 −46.960 1.00 36.83 O ATOM 4522 CG2 THR 566 44.680 35.060 −49.322 1.00 36.83 C ATOM 4523 C THR 566 47.060 32.934 −47.137 1.00 36.83 C ATOM 4524 O THR 566 48.022 33.674 −46.974 1.00 36.83 O ATOM 4525 N GLU 567 46.820 31.873 −46.362 1.00 36.83 N ATOM 4526 CA GLU 567 47.717 31.505 −45.264 1.00 36.83 C ATOM 4527 CB GLU 567 47.036 31.693 −43.896 1.00 36.83 C ATOM 4528 CG GLU 567 46.374 33.044 −43.647 1.00 36.83 C ATOM 4529 CD GLU 567 45.910 33.201 −42.213 1.00 36.83 C ATOM 4530 OE1 GLU 567 46.624 33.832 −41.411 1.00 36.83 O ATOM 4531 OE2 GLU 567 44.838 32.674 −41.865 1.00 36.83 O ATOM 4532 C GLU 567 48.221 30.060 −45.328 1.00 36.83 C ATOM 4533 O GLU 567 47.623 29.199 −45.973 1.00 36.83 O ATOM 4534 N PHE 568 49.345 29.815 −44.666 1.00 36.83 N ATOM 4535 CA PHE 568 49.908 28.474 −44.559 1.00 36.83 C ATOM 4536 CB PHE 568 50.971 28.180 −45.634 1.00 36.83 C ATOM 4537 CG PHE 568 52.230 28.978 −45.501 1.00 36.83 C ATOM 4538 CD1 PHE 568 52.367 30.201 −46.159 1.00 36.83 C ATOM 4539 CD2 PHE 568 53.288 28.506 −44.731 1.00 36.83 C ATOM 4540 CE1 PHE 568 53.543 30.941 −46.059 1.00 36.83 C ATOM 4541 CE2 PHE 568 54.467 29.234 −44.620 1.00 36.83 C ATOM 4542 CZ PHE 568 54.597 30.461 −45.290 1.00 36.83 C ATOM 4543 C PHE 568 50.524 28.408 −43.180 1.00 36.83 C ATOM 4544 O PHE 568 50.939 29.428 −42.648 1.00 36.83 O ATOM 4545 N GLY 569 50.555 27.223 −42.588 1.00 36.83 N ATOM 4546 CA GLY 569 51.131 27.088 −41.265 1.00 36.83 C ATOM 4547 C GLY 569 52.408 26.255 −41.216 1.00 36.83 C ATOM 4548 O GLY 569 52.613 25.354 −42.036 1.00 36.83 O ATOM 4549 N VAL 570 53.280 26.568 −40.265 1.00 36.83 N ATOM 4550 CA VAL 570 54.513 25.816 −40.088 1.00 36.83 C ATOM 4551 CB VAL 570 55.772 26.635 −40.472 1.00 36.83 C ATOM 4552 CG1 VAL 570 57.028 25.850 −40.105 1.00 36.83 C ATOM 4553 CG2 VAL 570 55.759 26.966 −41.972 1.00 36.83 C ATOM 4554 C VAL 570 54.600 25.438 −38.614 1.00 36.83 C ATOM 4555 O VAL 570 54.416 26.276 −37.746 1.00 36.83 O ATOM 4556 N THR 571 54.842 24.165 −38.339 1.00 36.83 N ATOM 4557 CA THR 571 54.953 23.709 −36.965 1.00 36.83 C ATOM 4558 CB THR 571 54.544 22.218 −36.842 1.00 36.83 C ATOM 4559 OG1 THR 571 53.173 22.069 −37.223 1.00 36.83 O ATOM 4560 CG2 THR 571 54.719 21.730 −35.416 1.00 36.83 C ATOM 4561 C THR 571 56.409 23.884 −36.517 1.00 36.83 C ATOM 4562 O THR 571 57.273 23.099 −36.910 1.00 36.83 O ATOM 4563 N HIS 572 56.664 24.925 −35.722 1.00 36.83 N ATOM 4564 CA HIS 572 58.004 25.237 −35.213 1.00 36.83 C ATOM 4565 CB HIS 572 58.162 26.751 −35.002 1.00 36.83 C ATOM 4566 CG HIS 572 58.192 27.549 −36.271 1.00 36.83 C ATOM 4567 CD2 HIS 572 57.238 28.299 −36.877 1.00 36.83 C ATOM 4568 ND1 HIS 572 59.313 27.646 −37.066 1.00 36.83 N ATOM 4569 CE1 HIS 572 59.051 28.424 −38.100 1.00 36.83 C ATOM 4570 NE2 HIS 572 57.799 28.834 −38.009 1.00 36.83 N ATOM 4571 C HIS 572 58.204 24.528 −33.881 1.00 36.83 C ATOM 4572 O HIS 572 57.250 24.028 −33.291 1.00 36.83 O ATOM 4573 N TYR 573 59.444 24.479 −33.414 1.00 36.83 N ATOM 4574 CA TYR 573 59.746 23.852 −32.135 1.00 36.83 C ATOM 4575 CB TYR 573 61.226 23.990 −31.796 1.00 36.83 C ATOM 4576 CG TYR 573 61.646 25.402 −31.431 1.00 36.83 C ATOM 4577 CD1 TYR 573 61.758 26.385 −32.405 1.00 36.83 C ATOM 4578 CE1 TYR 573 62.147 27.676 −32.088 1.00 36.83 C ATOM 4579 CD2 TYR 573 61.938 25.747 −30.108 1.00 36.83 C ATOM 4580 CE2 TYR 573 62.337 27.050 −29.776 1.00 36.83 C ATOM 4581 CZ TYR 573 62.438 28.010 −30.778 1.00 36.83 C ATOM 4582 OH TYR 573 62.823 29.300 −30.484 1.00 36.83 O ATOM 4583 C TYR 573 58.932 24.517 −31.025 1.00 36.83 C ATOM 4584 O TYR 573 58.552 23.867 −30.060 1.00 36.83 O ATOM 4585 N ALA 574 58.670 25.813 −31.169 1.00 36.83 N ATOM 4586 CA ALA 574 57.920 26.533 −30.160 1.00 36.83 C ATOM 4587 CB ALA 574 58.532 27.921 −29.942 1.00 36.83 C ATOM 4588 C ALA 574 56.427 26.647 −30.493 1.00 36.83 C ATOM 4589 O ALA 574 55.699 27.371 −29.828 1.00 36.83 O ATOM 4590 N GLY 575 55.985 25.925 −31.521 1.00 36.83 N ATOM 4591 CA GLY 575 54.588 25.950 −31.900 1.00 36.83 C ATOM 4592 C GLY 575 54.306 26.263 −33.359 1.00 36.83 C ATOM 4593 O GLY 575 55.174 26.708 −34.108 1.00 36.83 O ATOM 4594 N GLN 576 53.062 26.030 −33.754 1.00 36.83 N ATOM 4595 CA GLN 576 52.630 26.272 −35.113 1.00 36.83 C ATOM 4596 CB GLN 576 51.381 25.441 −35.438 1.00 36.83 C ATOM 4597 CG GLN 576 50.944 25.547 −36.898 1.00 36.83 C ATOM 4598 CD GLN 576 49.638 24.844 −37.158 1.00 36.83 C ATOM 4599 OE1 GLN 576 48.663 25.033 −36.431 1.00 36.83 O ATOM 4600 NE2 GLN 576 49.604 24.035 −38.200 1.00 36.83 N ATOM 4601 C GLN 576 52.323 27.742 −35.304 1.00 36.83 C ATOM 4602 O GLN 576 51.732 28.384 −34.441 1.00 36.83 O ATOM 4603 N VAL 577 52.737 28.260 −36.447 1.00 36.83 N ATOM 4604 CA VAL 577 52.518 29.644 −36.789 1.00 36.83 C ATOM 4605 CB VAL 577 53.844 30.439 −36.817 1.00 36.83 C ATOM 4606 CG1 VAL 577 53.573 31.890 −37.202 1.00 36.83 C ATOM 4607 CG2 VAL 577 54.512 30.377 −35.454 1.00 36.83 C ATOM 4608 C VAL 577 51.847 29.713 −38.152 1.00 36.83 C ATOM 4609 O VAL 577 52.285 29.087 −39.124 1.00 36.83 O ATOM 4610 N MET 578 50.764 30.465 −38.199 1.00 36.83 N ATOM 4611 CA MET 578 50.012 30.637 −39.415 1.00 36.83 C ATOM 4612 CB MET 578 48.506 30.720 −39.071 1.00 36.83 C ATOM 4613 CG MET 578 47.540 30.172 −40.123 1.00 36.83 C ATOM 4614 SD MET 578 47.910 28.522 −40.840 1.00 36.83 S ATOM 4615 CE MET 578 47.227 27.425 −39.701 1.00 36.83 C ATOM 4616 C MET 578 50.559 31.940 −40.008 1.00 36.83 C ATOM 4617 O MET 578 50.657 32.958 −39.319 1.00 36.83 O ATOM 4618 N TYR 579 50.945 31.885 −41.278 1.00 36.83 N ATOM 4619 CA TYR 579 51.508 33.033 −41.984 1.00 36.83 C ATOM 4620 CB TYR 579 52.891 32.659 −42.559 1.00 36.83 C ATOM 4621 CG TYR 579 53.950 32.353 −41.528 1.00 36.83 C ATOM 4622 CD1 TYR 579 54.642 33.376 −40.877 1.00 36.83 C ATOM 4623 CE1 TYR 579 55.604 33.090 −39.894 1.00 36.83 C ATOM 4624 CD2 TYR 579 54.244 31.039 −41.180 1.00 36.83 C ATOM 4625 CE2 TYR 579 55.194 30.743 −40.209 1.00 36.83 C ATOM 4626 CZ TYR 579 55.866 31.769 −39.569 1.00 36.83 C ATOM 4627 OH TYR 579 56.764 31.457 −38.590 1.00 36.83 O ATOM 4628 C TYR 579 50.620 33.562 −43.125 1.00 36.83 C ATOM 4629 O TYR 579 50.018 32.790 −43.863 1.00 36.83 O ATOM 4630 N GLU 580 50.559 34.887 −43.258 1.00 36.83 N ATOM 4631 CA GLU 580 49.801 35.549 −44.317 1.00 36.83 C ATOM 4632 CB GLU 580 49.223 36.870 −43.804 1.00 36.83 C ATOM 4633 CG GLU 580 48.549 37.737 −44.862 1.00 36.83 C ATOM 4634 CD GLU 580 47.559 36.976 −45.720 1.00 26.83 C ATOM 4635 OE1 GLU 580 46.684 36.274 −45.167 1.00 36.83 O ATOM 4636 OE2 GLU 580 47.653 37.086 −46.959 1.00 36.83 O ATOM 4637 C GLU 580 50.782 35.791 −45.465 1.00 36.83 C ATOM 4638 O GLU 580 51.864 36.333 −45.254 1.00 36.83 O ATOM 4639 N ILE 581 50.402 35.397 −46.679 1.00 36.83 N ATOM 4640 CA ILE 581 51.287 35.520 −47.842 1.00 36.83 C ATOM 4641 CB ILE 581 50.952 34.418 −48.893 1.00 36.83 C ATOM 4642 CG2 ILE 581 49.843 34.900 −49.857 1.00 36.83 C ATOM 4643 CG1 ILE 581 52.198 34.069 −49.712 1.00 36.83 C ATOM 4644 CD1 ILE 581 53.265 33.316 −48.946 1.00 36.83 C ATOM 4645 C ILE 581 51.273 36.882 −48.548 1.00 36.83 C ATOM 4646 O ILE 581 52.134 37.163 −49.383 1.00 36.83 O ATOM 4647 N GLN 582 50.301 37.721 −48.207 1.00 36.83 N ATOM 4648 CA GLN 582 50.161 39.024 −48.846 1.00 36.83 C ATOM 4649 CB GLN 582 49.030 39.810 −48.178 1.00 36.83 C ATOM 4650 CG GLN 582 48.703 41.132 −48.844 1.00 36.83 C ATOM 4651 CD GLN 582 47.963 42.079 −47.909 1.00 36.83 C ATOM 4652 OE1 GLN 582 46.813 41.829 −47.531 1.00 36.83 O ATOM 4653 NE2 GLN 582 48.629 43.171 −47.519 1.00 36.83 N ATOM 4654 C GLN 582 51.443 39.852 −48.846 1.00 36.83 C ATOM 4655 O GLN 582 52.053 40.056 −47.806 1.00 36.83 O ATOM 4656 N ASP 583 51.845 40.303 −50.036 1.00 36.83 N ATOM 4657 CA ASP 583 53.026 41.136 −50.228 1.00 36.83 C ATOM 4658 CB ASP 583 53.012 42.278 −49.210 1.00 36.83 C ATOM 4659 CG ASP 583 52.069 43.394 −49.608 1.00 36.83 C ATOM 4660 OD1 ASP 583 51.519 44.060 −48.708 1.00 36.83 O ATOM 4661 OD2 ASP 583 51.889 43.616 −50.829 1.00 36.83 O ATOM 4662 C ASP 583 54.388 40.462 −50.200 1.00 36.83 C ATOM 4663 O ASP 583 55.403 41.134 −50.357 1.00 36.83 O ATOM 4664 N TRP 584 54.429 39.152 −50.006 1.00 36.83 N ATOM 4665 CA TRP 584 55.707 38.450 −49.942 1.00 36.83 C ATOM 4666 CB TRP 584 55.478 36.956 −49.669 1.00 36.83 C ATOM 4667 CG TRP 584 55.232 36.694 −48.216 1.00 36.83 C ATOM 4668 CD2 TRP 584 55.654 35.558 −47.462 1.00 36.83 C ATOM 4669 CE2 TRP 584 55.207 35.748 −46.141 1.00 36.83 C ATOM 4670 CE3 TRP 584 56.367 34.397 −47.774 1.00 36.83 C ATOM 4671 CD1 TRP 584 54.565 37.503 −47.344 1.00 36.83 C ATOM 4672 NE1 TRP 584 54.548 36.946 −46.102 1.00 36.83 N ATOM 4673 CZ2 TRP 584 55.451 34.822 −45.127 1.00 36.83 C ATOM 4674 CZ3 TRP 584 56.612 33.471 −46.765 1.00 36.83 C ATOM 4675 CH2 TRP 584 56.154 33.690 −45.457 1.00 36.83 C ATOM 4676 C TRP 584 56.592 38.642 −51.175 1.00 36.83 C ATOM 4677 O TRP 584 57.809 38.785 −51.056 1.00 36.83 O ATOM 4678 N LEU 585 55.988 38.653 −52.353 1.00 36.83 N ATOM 4679 CA LEU 585 56.771 38.840 −53.558 1.00 36.83 C ATOM 4680 CB LEU 585 55.878 38.751 −54.798 1.00 36.83 C ATOM 4681 CG LEU 585 55.252 37.368 −55.036 1.00 36.83 C ATOM 4682 CD1 LEU 585 54.484 37.386 −56.347 1.00 36.83 C ATOM 4683 CD2 LEU 585 56.337 36.300 −55.063 1.00 36.83 C ATOM 4684 C LEU 585 57.498 40.178 −53.508 1.00 36.83 C ATOM 4685 O LEU 585 58.699 40.239 −53.728 1.00 36.83 O ATOM 4686 N GLU 586 56.777 41.243 −53.191 1.00 36.83 N ATOM 4687 CA GLU 586 57.396 42.564 −53.120 1.00 36.83 C ATOM 4688 CB GLU 586 56.320 43.657 −53.080 1.00 36.83 C ATOM 4689 CG GLU 586 55.432 43.684 −54.313 1.00 36.83 C ATOM 4690 CD GLU 586 56.169 44.076 −55.588 1.00 36.83 C ATOM 4691 OE1 GLU 586 56.732 45.198 −55.622 1.00 36.83 O ATOM 4692 OE2 GLU 586 56.174 43.271 −56.550 1.00 36.83 O ATOM 4693 C GLU 586 58.350 42.736 −51.933 1.00 36.83 C ATOM 4694 O GLU 586 59.317 43.491 −52.015 1.00 36.83 O ATOM 4695 N LYS 587 58.085 42.058 −50.826 1.00 36.83 N ATOM 4696 CA LYS 587 58.976 42.174 −49.686 1.00 36.83 C ATOM 4697 CB LYS 587 58.334 41.588 −48.427 1.00 36.83 C ATOM 4698 CG LYS 587 57.260 42.484 −47.813 1.00 36.83 C ATOM 4699 CD LYS 587 56.727 41.948 −46.488 1.00 36.83 C ATOM 4700 CE LYS 587 55.866 42.998 −45.813 1.00 36.83 C ATOM 4701 NZ LYS 587 55.285 42.573 −44.510 1.00 36.83 N ATOM 4702 C LYS 587 60.270 41.435 −50.011 1.00 36.83 C ATOM 4703 O LYS 587 61.349 41.881 −49.646 1.00 36.83 O ATOM 4704 N ASN 588 60.163 40.312 −50.715 1.00 36.83 N ATOM 4705 CA ASN 588 61.356 39.553 −51.057 1.00 36.83 C ATOM 4706 CB ASN 588 60.994 38.105 −51.411 1.00 36.83 C ATOM 4707 CG ASN 588 62.224 37.206 −51.509 1.00 36.83 C ATOM 4708 OD1 ASN 588 62.994 37.096 −50.560 1.00 36.83 O ATOM 4709 ND2 ASN 588 62.413 36.572 −52.663 1.00 36.83 N ATOM 4710 C ASN 588 62.168 40.198 −52.201 1.00 36.83 C ATOM 4711 O ASN 588 63.371 39.994 −52.286 1.00 36.83 O ATOM 4712 N LYS 589 61.515 40.969 −53.069 1.00 36.83 N ATOM 4713 CA LYS 589 62.218 41.633 −54.170 1.00 36.83 C ATOM 4714 CB LYS 589 61.274 41.859 −55.356 1.00 36.83 C ATOM 4715 CG LYS 589 60.657 40.582 −55.945 1.00 36.83 C ATOM 4716 CD LYS 589 59.823 40.876 −57.201 1.00 36.83 C ATOM 4717 CE LYS 589 58.778 41.986 −56.956 1.00 36.83 C ATOM 4718 NZ LYS 589 57.927 42.318 −58.163 1.00 36.83 N ATOM 4719 C LYS 589 62.793 42.984 −53.695 1.00 36.83 C ATOM 4720 O LYS 589 63.749 43.493 −54.259 1.00 36.83 O ATOM 4721 N ASP 590 62.187 43.560 −52.661 1.00 36.83 N ATOM 4722 CA ASP 590 62.652 44.821 −52.096 1.00 36.83 C ATOM 4723 CB ASP 590 63.890 44.559 −51.227 1.00 36.83 C ATOM 4724 CG ASP 590 64.189 45.691 −50.257 1.00 36.83 C ATOM 4725 OD1 ASP 590 65.347 45.792 −49.807 1.00 36.83 O ATOM 4726 OD2 ASP 590 63.272 46.468 −49.926 1.00 36.83 O ATOM 4727 C ASP 590 62.995 45.858 −53.172 1.00 36.83 C ATOM 4728 O ASP 590 64.109 46.351 −53.217 1.00 36.83 O ATOM 4729 N PRO 591 62.037 46.196 −54.052 1.00 36.83 N ATOM 4730 CD PRO 591 60.724 45.560 −54.256 1.00 36.83 C ATOM 4731 CA PRO 591 62.304 47.183 −55.106 1.00 36.83 C ATOM 4732 CB PRO 591 61.220 46.887 −56.128 1.00 36.83 C ATOM 4733 CG PRO 591 60.069 46.478 −55.256 1.00 36.83 C ATOM 4734 C PRO 591 62.294 48.655 −54.677 1.00 36.83 C ATOM 4735 O PRO 591 61.805 49.014 −53.612 1.00 36.83 O ATOM 4736 N LEU 592 62.856 49.488 −55.541 1.00 36.83 N ATOM 4737 CA LEU 592 62.939 50.933 −55.357 1.00 36.83 C ATOM 4738 CB LEU 592 64.094 51.293 −54.417 1.00 36.83 C ATOM 4739 CG LEU 592 64.320 52.778 −54.090 1.00 36.83 C ATOM 4740 CD1 LEU 592 63.094 53.343 −53.373 1.00 36.83 C ATOM 4741 CD2 LEU 592 65.567 52.934 −53.211 1.00 36.83 C ATOM 4742 C LEU 592 63.188 51.552 −56.740 1.00 36.83 C ATOM 4743 O LEU 592 64.079 51.118 −57.471 1.00 36.83 O ATOM 4744 N GLN 593 62.388 52.548 −57.108 1.00 36.83 N ATOM 4745 CA GLN 593 62.566 53.203 −58.401 1.00 36.83 C ATOM 4746 CB GLN 593 61.519 54.299 −58.596 1.00 36.83 C ATOM 4747 CG GLN 593 60.143 53.774 −58.931 1.00 36.83 C ATOM 4748 CD GLN 593 60.159 52.835 −60.115 1.00 36.83 C ATOM 4749 OE1 GLN 593 61.030 52.922 −60.983 1.00 36.83 O ATOM 4750 NE2 GLN 593 59.187 51.942 −60.167 1.00 36.83 N ATOM 4751 C GLN 593 63.964 53.811 −58.523 1.00 36.83 C ATOM 4752 O GLN 593 64.413 54.517 −57.623 1.00 36.83 O ATOM 4753 N GLN 594 64.649 53.534 −59.634 1.00 36.83 N ATOM 4754 CA GLN 594 65.987 54.080 −59.836 1.00 36.83 C ATOM 4755 CB GLN 594 66.610 53.595 −61.159 1.00 36.83 C ATOM 4756 CG GLN 594 67.042 52.130 −61.119 1.00 36.83 C ATOM 4757 CD GLN 594 67.889 51.703 −62.312 1.00 36.83 C ATOM 4758 OE1 GLN 594 69.090 52.001 −62.386 1.00 36.83 O ATOM 4759 NE2 GLN 594 67.265 51.000 −63.258 1.00 36.83 N ATOM 4760 C GLN 594 65.913 55.594 −59.806 1.00 36.83 C ATOM 4761 O GLN 594 66.823 56.240 −59.318 1.00 36.83 O ATOM 4762 N ASP 595 64.822 56.162 −60.311 1.00 36.83 N ATOM 4763 CA ASP 595 64.665 57.615 −60.288 1.00 36.83 C ATOM 4764 CB ASP 595 63.371 58.025 −60.992 1.00 36.83 C ATOM 4765 CG ASP 595 63.587 58.353 −62.460 1.00 36.83 C ATOM 4766 OD1 ASP 595 64.677 58.044 −62.995 1.00 36.83 O ATOM 4767 OD2 ASP 595 62.663 58.919 −63.075 1.00 36.83 O ATOM 4768 C ASP 595 64.684 58.148 −58.853 1.00 36.83 C ATOM 4769 O ASP 595 65.103 59.278 −58.601 1.00 36.83 O ATOM 4770 N LEU 596 64.240 57.336 −57.900 1.00 36.83 N ATOM 4771 CA LEU 596 64.265 57.790 −56.515 1.00 36.83 C ATOM 4772 CB LEU 596 63.396 56.893 −55.635 1.00 36.83 C ATOM 4773 CG LEU 596 61.915 57.161 −55.906 1.00 36.83 C ATOM 4774 CD1 LEU 596 61.046 56.057 −55.320 1.00 36.83 C ATOM 4775 CD2 LEU 596 61.553 58.524 −55.330 1.00 36.83 C ATOM 4776 C LEU 596 65.713 57.812 −56.048 1.00 36.83 C ATOM 4777 O LEU 596 66.145 58.763 −55.400 1.00 36.83 O ATOM 4778 N GLU 597 66.468 56.779 −56.416 1.00 36.83 N ATOM 4779 CA GLU 597 67.882 56.705 −56.053 1.00 36.83 C ATOM 4780 CB GLU 597 68.465 55.338 −56.437 1.00 36.83 C ATOM 4781 CG GLU 597 68.262 54.241 −55.375 1.00 36.83 C ATOM 4782 CD GLU 597 68.763 52.868 −55.822 1.00 36.83 C ATOM 4783 OE1 GLU 597 68.110 52.263 −56.701 1.00 36.83 O ATOM 4784 OE2 GLU 597 69.810 52.391 −55.301 1.00 36.83 O ATOM 4785 C GLU 597 68.678 57.842 −56.722 1.00 36.83 C ATOM 4786 O GLU 597 69.614 58.378 −56.126 1.00 36.83 O ATOM 4787 N LEU 598 68.303 58.211 −57.950 1.00 36.83 N ATOM 4788 CA LEU 598 68.976 59.292 −58.666 1.00 36.83 C ATOM 4789 CB LEU 598 68.456 59.410 −60.096 1.00 36.83 C ATOM 4790 CG LEU 598 68.895 58.335 −61.077 1.00 36.83 C ATOM 4791 CD1 LEU 598 68.059 58.441 −62.340 1.00 36.83 C ATOM 4792 CD2 LEU 598 70.397 58.489 −61.365 1.00 36.83 C ATOM 4793 C LEU 598 68.731 60.615 −57.956 1.00 36.83 C ATOM 4794 O LEU 598 69.664 61.385 −57.727 1.00 36.83 O ATOM 4795 N CYS 599 67.465 60.866 −57.625 1.00 36.83 N ATOM 4796 CA CYS 599 67.071 62.085 −56.945 1.00 36.83 C ATOM 4797 CB CYS 599 65.558 62.108 −56.758 1.00 36.83 C ATOM 4798 SG CYS 599 65.021 63.046 −55.325 1.00 36.83 S ATOM 4799 C CYS 599 67.753 62.261 −55.598 1.00 36.83 C ATOM 4800 O CYS 599 67.969 63.394 −55.149 1.00 36.83 O ATOM 4801 N PHE 600 68.094 61.150 −54.948 1.00 36.83 N ATOM 4802 CA PHE 600 68.749 61.241 −53.652 1.00 36.83 C ATOM 4803 CB PHE 600 68.249 60.146 −52.699 1.00 36.83 C ATOM 4804 CG PHE 600 67.009 60.537 −51.944 1.00 36.83 C ATOM 4805 CD1 PHE 600 65.756 60.466 −52.548 1.00 36.83 C ATOM 4806 CD2 PHE 600 67.102 61.047 −50.650 1.00 36.83 C ATOM 4807 CE1 PHE 600 64.620 60.900 −51.884 1.00 36.83 C ATOM 4808 CE2 PHE 600 65.967 61.484 −49.974 1.00 36.83 C ATOM 4809 CZ PHE 600 64.720 61.414 −50.592 1.00 36.83 C ATOM 4810 C PHE 600 70.270 61.269 −53.673 1.00 36.83 C ATOM 4811 O PHE 600 70.877 61.771 −52.738 1.00 36.83 O ATOM 4812 N LYS 601 70.896 60.743 −54.718 1.00 36.83 N ATOM 4813 CA LYS 601 72.363 60.804 −54.785 1.00 36.83 C ATOM 4814 CB LYS 601 72.915 60.041 −55.997 1.00 36.83 C ATOM 4815 CG LYS 601 72.866 58.516 −55.880 1.00 36.83 C ATOM 4816 CD LYS 601 73.502 57.806 −57.095 1.00 36.83 C ATOM 4817 CE LYS 601 73.304 56.285 −56.993 1.00 36.83 C ATOM 4818 NZ LYS 601 74.186 55.465 −57.887 1.00 36.83 N ATOM 4819 C LYS 601 72.771 62.276 −54.903 1.00 36.83 C ATOM 4820 O LYS 601 73.873 62.647 −54.515 1.00 36.83 O ATOM 4821 N ASP 602 71.879 63.102 −55.449 1.00 36.83 N ATOM 4822 CA ASP 602 72.150 64.534 −55.619 1.00 36.83 C ATOM 4823 CB ASP 602 71.353 65.098 −56.796 1.00 36.83 C ATOM 4824 CG ASP 602 71.788 64.531 −58.122 1.00 36.83 C ATOM 4825 OD1 ASP 602 71.040 64.719 −59.104 1.00 36.83 O ATOM 4826 OD2 ASP 602 72.872 63.908 −58.187 1.00 36.83 O ATOM 4827 C ASP 602 71.788 65.343 −54.377 1.00 36.83 C ATOM 4828 O ASP 602 71.604 66.558 −54.460 1.00 36.83 O ATOM 4829 N SER 603 71.657 64.674 −53.237 1.00 36.83 N ATOM 4830 CA SER 603 71.322 65.363 −52.000 1.00 36.83 C ATOM 4831 CB SER 603 71.000 64.351 −50.901 1.00 36.83 C ATOM 4832 OG SER 603 70.838 64.987 −49.640 1.00 36.83 O ATOM 4833 C SER 603 72.480 66.241 −51.542 1.00 36.83 C ATOM 4834 O SER 603 73.647 65.867 −51.675 1.00 36.83 O ATOM 4835 N SER 604 72.153 67.408 −50.994 1.00 36.83 N ATOM 4836 CA SER 604 73.180 68.313 −50.506 1.00 36.83 C ATOM 4837 CB SER 604 72.621 69.737 −50.339 1.00 36.83 C ATOM 4838 OG SER 604 71.202 69.764 −50.197 1.00 36.83 O ATOM 4839 C SER 604 73.744 67.805 −49.189 1.00 36.83 C ATOM 4840 O SER 604 74.907 68.070 −48.864 1.00 36.83 O ATOM 4841 N ASP 605 72.935 67.047 −48.446 1.00 36.83 N ATOM 4842 CA ASP 605 73.368 66.513 −47.159 1.00 36.83 C ATOM 4843 CB ASP 605 72.180 65.957 −46.355 1.00 36.83 C ATOM 4844 CG ASP 605 72.543 65.670 −44.888 1.00 36.83 C ATOM 4845 OD1 ASP 605 72.324 66.561 −44.031 1.00 36.83 O ATOM 4846 OD2 ASP 605 73.071 64.562 −44.595 1.00 36.83 O ATOM 4847 C ASP 605 74.437 65.433 −47.292 1.00 36.83 C ATOM 4848 O ASP 605 74.302 64.457 −48.041 1.00 36.83 O ATOM 4849 N ASN 606 75.501 65.620 −46.530 1.00 36.83 N ATOM 4850 CA ASN 606 76.629 64.711 −46.507 1.00 36.83 C ATOM 4851 CB ASN 606 77.681 65.256 −45.532 1.00 36.83 C ATOM 4852 CG ASN 606 78.858 64.331 −45.369 1.00 36.83 C ATOM 4853 OD1 ASN 606 79.593 64.415 −44.375 1.00 36.83 O ATOM 4854 ND2 ASN 606 79.061 63.449 −46.342 1.00 36.83 N ATOM 4855 C ASN 606 76.227 63.283 −46.114 1.00 36.83 C ATOM 4856 O ASN 606 76.743 62.314 −46.677 1.00 36.83 O ATOM 4857 N VAL 607 75.313 63.149 −45.152 1.00 36.83 N ATOM 4858 CA VAL 607 74.872 61.830 −44.716 1.00 36.83 C ATOM 4859 CB VAL 607 74.184 61.927 −43.342 1.00 36.83 C ATOM 4860 CG1 VAL 607 73.472 60.627 −42.990 1.00 36.83 C ATOM 4861 CG2 VAL 607 75.244 62.228 −42.281 1.00 36.83 C ATOM 4862 C VAL 607 73.969 61.158 −45.751 1.00 36.83 C ATOM 4863 O VAL 607 74.223 60.017 −46.154 1.00 36.83 O ATOM 4864 N VAL 608 72.938 61.865 −46.203 1.00 36.83 N ATOM 4865 CA VAL 608 72.014 61.332 −47.205 1.00 36.83 C ATOM 4866 CB VAL 608 70.985 62.420 −47.613 1.00 36.83 C ATOM 4867 CG1 VAL 608 70.095 61.919 −48.720 1.00 36.83 C ATOM 4868 CG2 VAL 608 70.145 62.820 −46.408 1.00 36.83 C ATOM 4869 C VAL 608 72.739 60.797 −48.466 1.00 36.83 C ATOM 4870 O VAL 608 72.334 59.780 −49.049 1.00 36.83 O ATOM 4871 N THR 609 73.817 61.464 −48.872 1.00 36.83 N ATOM 4872 CA THR 609 74.580 61.068 −50.062 1.00 36.83 C ATOM 4873 CB THR 609 75.602 62.138 −50.473 1.00 36.83 C ATOM 4874 OG1 THR 609 74.926 63.380 −50.696 1.00 36.83 O ATOM 4875 CG2 THR 609 76.307 61.733 −51.748 1.00 36.83 C ATOM 4876 C THR 609 75.349 59.780 −49.869 1.00 36.83 C ATOM 4877 O THR 609 75.499 58.990 −50.807 1.00 36.83 O ATOM 4878 N LYS 610 75.862 59.579 −48.664 1.00 36.83 N ATOM 4879 CA LYS 610 76.614 58.369 −48.373 1.00 36.83 C ATOM 4880 CB LYS 610 77.219 58.443 −46.972 1.00 36.83 C ATOM 4881 CG LYS 610 78.435 57.571 −46.789 1.00 36.83 C ATOM 4882 CD LYS 610 79.712 58.403 −46.818 1.00 36.83 C ATOM 4883 CE LYS 610 80.374 58.431 −45.429 1.00 36.83 C ATOM 4884 NZ LYS 610 80.719 57.043 −44.950 1.00 36.83 N ATOM 4885 C LYS 610 75.678 57.156 −48.453 1.00 36.83 C ATOM 4886 O LYS 610 76.098 56.058 −48.813 1.00 36.83 O ATOM 4887 N LEU 611 74.406 57.362 −48.117 1.00 36.83 N ATOM 4888 CA LEU 611 73.448 56.265 −48.145 1.00 36.83 C ATOM 4889 CB LEU 611 72.219 56.608 −47.297 1.00 36.83 C ATOM 4890 CG LEU 611 72.590 56.911 −45.841 1.00 36.83 C ATOM 4891 CD1 LEU 611 71.333 56.920 −44.988 1.00 36.83 C ATOM 4892 CD2 LEU 611 73.583 55.876 −45.324 1.00 36.83 C ATOM 4893 C LEU 611 73.033 55.865 −49.554 1.00 36.83 C ATOM 4894 O LEU 611 72.569 54.757 −49.765 1.00 36.83 O ATOM 4895 N PHE 612 73.224 56.760 −50.517 1.00 36.83 N ATOM 4896 CA PHE 612 72.873 56.472 −51.905 1.00 36.83 C ATOM 4897 CB PHE 612 71.854 57.502 −52.400 1.00 36.83 C ATOM 4898 CG PHE 612 70.520 57.409 −51.720 1.00 36.83 C ATOM 4899 CD1 PHE 612 70.299 58.033 −50.490 1.00 36.83 C ATOM 4900 CD2 PHE 612 69.465 56.724 −52.329 1.00 36.83 C ATOM 4901 CE1 PHE 612 69.053 57.988 −49.879 1.00 36.83 C ATOM 4902 CE2 PHE 612 68.199 56.668 −51.724 1.00 36.83 C ATOM 4903 CZ PHE 612 67.993 57.306 −50.496 1.00 36.83 C ATOM 4904 C PHE 612 74.061 56.378 −52.892 1.00 36.83 C ATOM 4905 O PHE 612 73.863 56.205 −54.094 1.00 36.83 O ATOM 4906 N ASN 613 75.286 56.462 −52.374 1.00 36.83 N ATOM 4907 CA ASN 613 76.506 56.373 −53.179 1.00 36.83 C ATOM 4908 CB ASN 613 77.251 57.713 −53.155 1.00 36.83 C ATOM 4909 CG ASN 613 76.794 58.657 −54.247 1.00 36.83 C ATOM 4910 OD1 ASN 613 77.131 58.476 −55.415 1.00 36.83 O ATOM 4911 ND2 ASN 613 76.015 59.666 −53.877 1.00 36.83 N ATOM 4912 C ASN 613 77.439 55.260 −52.669 1.00 36.83 C ATOM 4913 O ASN 613 78.019 54.505 −53.449 1.00 36.83 O ATOM 4914 N ASP 614 77.599 55.171 −51.354 1.00 36.83 N ATOM 4915 CA ASP 614 78.447 54.144 −50.764 1.00 36.83 C ATOM 4916 CB ASP 614 78.310 54.158 −49.240 1.00 36.83 C ATOM 4917 CG ASP 614 79.303 53.236 −48.557 1.00 36.83 C ATOM 4918 OD1 ASP 614 79.374 52.034 −48.909 1.00 36.83 O ATOM 4919 OD2 ASP 614 80.018 53.718 −47.654 1.00 36.83 O ATOM 4920 C ASP 614 78.028 52.766 −51.283 1.00 36.83 C ATOM 4921 O ASP 614 76.930 52.286 −50.996 1.00 36.83 O ATOM 4922 N PRO 615 78.912 52.109 −52.040 1.00 36.83 N ATOM 4923 CD PRO 615 80.324 52.502 −52.218 1.00 36.83 C ATOM 4924 CA PRO 615 78.665 50.780 −52.611 1.00 36.83 C ATOM 4925 CB PRO 615 79.975 50.475 −53.327 1.00 36.83 C ATOM 4926 CG PRO 615 80.998 51.164 −52.437 1.00 36.83 C ATOM 4927 C PRO 615 78.345 49.746 −51.527 1.00 36.83 C ATOM 4928 O PRO 615 77.604 48.781 −51.755 1.00 36.83 O ATOM 4929 N ASN 616 78.902 49.950 −50.342 1.00 36.83 N ATOM 4930 CA ASN 616 78.657 49.017 −49.248 1.00 36.83 C ATOM 4931 CB ASN 616 79.874 48.931 −48.328 1.00 36.83 C ATOM 4932 CG ASN 616 81.063 48.296 −49.007 1.00 36.83 C ATOM 4933 OD1 ASN 616 80.904 47.491 −49.937 1.00 36.83 O ATOM 4934 ND2 ASN 616 82.267 48.635 −48.541 1.00 36.83 N ATOM 4935 C ASN 616 77.426 49.367 −48.422 1.00 36.83 C ATOM 4936 O ASN 616 77.300 48.914 −47.284 1.00 36.83 O ATOM 4937 N ILE 617 76.518 50.157 −48.997 1.00 36.83 N ATOM 4938 CA ILE 617 75.299 50.556 −48.299 1.00 36.83 C ATOM 4939 CB ILE 617 75.472 51.932 −47.619 1.00 36.83 C ATOM 4940 CG2 ILE 617 74.138 52.406 −47.079 1.00 36.83 C ATOM 4941 CG1 ILE 617 76.536 51.839 −46.513 1.00 36.83 C ATOM 4942 CD1 ILE 617 76.764 53.120 −45.759 1.00 36.83 C ATOM 4943 C ILE 617 74.103 50.643 −49.245 1.00 36.83 C ATOM 4944 O ILE 617 72.999 50.211 −48.903 1.00 36.83 O ATOM 4945 N ALA 618 74.330 51.201 −50.432 1.00 36.83 N ATOM 4946 CA ALA 618 73.272 51.374 −51.420 1.00 36.83 C ATOM 4947 CB ALA 618 73.171 52.855 −51.808 1.00 36.83 C ATOM 4948 C ALA 618 73.424 50.520 −52.683 1.00 36.83 C ATOM 4949 O ALA 618 72.751 50.774 −53.690 1.00 36.83 O ATOM 4950 N SER 619 74.294 49.513 −52.642 1.00 36.83 N ATOM 4951 CA SER 619 74.483 48.661 −53.809 1.00 36.83 C ATOM 4952 CB SER 619 75.937 48.202 −53.903 1.00 36.83 C ATOM 4953 OG SER 619 76.217 47.708 −55.201 1.00 36.83 O ATOM 4954 C SER 619 73.564 47.456 −53.706 1.00 36.83 C ATOM 4955 O SER 619 72.787 47.354 −52.770 1.00 36.83 O ATOM 4956 N ARG 620 73.648 46.536 −54.658 1.00 36.83 N ATOM 4957 CA ARG 620 72.781 45.355 −54.631 1.00 36.83 C ATOM 4958 CB ARG 620 71.393 45.699 −55.203 1.00 36.83 C ATOM 4959 CG ARG 620 70.483 46.501 −54.287 1.00 36.83 C ATOM 4960 CD ARG 620 69.749 45.597 −53.289 1.00 36.83 C ATOM 4961 NE ARG 620 68.959 44.560 −53.964 1.00 36.83 N ATOM 4962 CZ ARG 620 68.160 43.699 −53.339 1.00 36.83 C ATOM 4963 NH1 ARG 620 68.033 43.748 −52.015 1.00 36.83 N ATOM 4964 NH2 ARG 620 67.497 42.784 −54.037 1.00 36.83 N ATOM 4965 C ARG 620 73.370 44.216 −55.444 1.00 36.83 C ATOM 4966 O ARG 620 73.562 44.358 −56.649 1.00 36.83 O ATOM 4967 N ALA 621 73.612 43.082 −54.793 1.00 36.83 N ATOM 4968 CA ALA 621 74.175 41.894 −55.442 1.00 36.83 C ATOM 4969 CB ALA 621 74.350 40.790 −54.402 1.00 36.83 C ATOM 4970 C ALA 621 73.347 41.360 −56.613 1.00 36.83 C ATOM 4971 O ALA 621 72.116 41.260 −56.515 1.00 36.83 O ATOM 4972 N LYS 622 74.023 41.001 −57.707 1.00 36.83 N ATOM 4973 CA LYS 622 73.365 40.460 −58.898 1.00 36.83 C ATOM 4974 CB LYS 622 74.137 40.857 −60.163 1.00 36.83 C ATOM 4975 CG LYS 622 74.221 42.359 −60.423 1.00 36.83 C ATOM 4976 CD LYS 622 75.642 42.768 −60.823 1.00 36.83 C ATOM 4977 CE LYS 622 76.574 42.906 −59.607 1.00 36.83 C ATOM 4978 NZ LYS 622 76.294 44.132 −58.778 1.00 36.83 N ATOM 4979 C LYS 622 73.288 38.928 −58.831 1.00 36.83 C ATOM 4980 O LYS 622 74.272 38.233 −59.097 1.00 36.83 O ATOM 4981 N LYS 623 72.126 38.395 −58.477 1.00 36.83 N ATOM 4982 CA LYS 623 71.975 36.946 −58.393 1.00 36.83 C ATOM 4983 CB LYS 623 70.898 36.572 −57.369 1.00 36.83 C ATOM 4984 CG LYS 623 70.552 35.067 −57.332 1.00 36.83 C ATOM 4985 CD LYS 623 71.590 34.248 −56.579 1.00 36.83 C ATOM 4986 CE LYS 623 71.303 34.246 −55.082 1.00 36.83 C ATOM 4987 NZ LYS 623 70.017 33.531 −54.779 1.00 36.83 N ATOM 4988 C LYS 623 71.574 36.500 −59.776 1.00 36.83 C ATOM 4989 O LYS 623 70.450 36.027 −60.001 1.00 36.83 O ATOM 4990 N GLY 624 72.500 36.665 −60.713 1.00 36.83 N ATOM 4991 CA GLY 624 72.219 36.304 −62.088 1.00 36.83 C ATOM 4992 C GLY 624 71.757 37.546 −62.827 1.00 36.83 C ATOM 4993 O GLY 624 72.478 38.549 −62.858 1.00 36.83 O ATOM 4994 N ALA 625 70.558 37.479 −63.407 1.00 36.83 N ATOM 4995 CA ALA 625 69.961 38.583 −64.161 1.00 36.83 C ATOM 4996 CB ALA 625 69.101 38.023 −65.303 1.00 36.83 C ATOM 4997 C ALA 625 69.115 39.516 −63.284 1.00 36.83 C ATOM 4998 O ALA 625 68.669 40.571 −63.736 1.00 36.83 O ATOM 4999 N ASN 626 68.883 39.116 −62.037 1.00 36.83 N ATOM 5000 CA ASN 626 68.112 39.924 −61.104 1.00 36.83 C ATOM 5001 CB ASN 626 66.825 39.197 −60.694 1.00 36.83 C ATOM 5002 CG ASN 626 65.914 38.911 −61.869 1.00 36.83 C ATOM 5003 OD1 ASN 626 65.399 39.838 −62.511 1.00 36.83 O ATOM 5004 ND2 ASN 626 65.712 37.618 −62.166 1.00 36.83 N ATOM 5005 C ASN 626 68.910 40.222 −59.835 1.00 36.83 C ATOM 5006 O ASN 626 69.998 39.663 −59.596 1.00 36.83 O ATOM 5007 N PHE 627 68.334 41.092 −59.009 1.00 36.83 N ATOM 5008 CA PHE 627 68.938 41.463 −57.742 1.00 36.83 C ATOM 5009 CB PHE 627 68.262 42.719 −57.182 1.00 36.83 C ATOM 5010 CG PHE 627 68.557 43.974 −57.966 1.00 36.83 C ATOM 5011 CD1 PHE 627 69.880 44.388 −58.180 1.00 36.83 C ATOM 5012 CD2 PHE 627 67.513 44.762 −58.471 1.00 36.83 C ATOM 5013 CE1 PHE 627 70.160 45.569 −58.882 1.00 36.83 C ATOM 5014 CE2 PHE 627 67.782 45.948 −59.178 1.00 36.83 C ATOM 5015 CZ PHE 627 69.105 46.352 −59.383 1.00 36.83 C ATOM 5016 C PHE 627 68.748 40.295 −56.781 1.00 36.83 C ATOM 5017 O PHE 627 67.717 39.618 −56.818 1.00 36.83 O ATOM 5018 N ILE 628 69.750 40.043 −55.937 1.00 36.83 N ATOM 5019 CA ILE 628 69.648 38.953 −54.969 1.00 36.83 C ATOM 5020 CB ILE 628 70.910 38.875 −54.050 1.00 36.83 C ATOM 5021 CG2 ILE 628 71.013 40.118 −53.164 1.00 36.83 C ATOM 5022 CG1 ILE 628 70.847 37.619 −53.181 1.00 36.83 C ATOM 5023 CD1 ILE 628 72.084 37.413 −52.306 1.00 36.83 C ATOM 5024 C ILE 628 68.402 39.214 −54.120 1.00 36.83 C ATOM 5025 O ILE 628 68.124 40.356 −53.760 1.00 36.83 O ATOM 5026 N THR 629 67.647 38.166 −53.809 1.00 36.83 N ATOM 5027 CA THR 629 66.449 38.355 −53.007 1.00 36.83 C ATOM 5028 CB THR 629 65.477 37.179 −53.152 1.00 36.83 C ATOM 5029 OG1 THR 629 66.074 35.983 −52.635 1.00 36.83 O ATOM 5030 CG2 THR 629 65.111 36.985 −54.604 1.00 36.83 C ATOM 5031 C THR 629 66.798 38.513 −51.538 1.00 36.83 C ATOM 5032 O THR 629 67.865 38.066 −51.091 1.00 36.83 O ATOM 5033 N VAL 630 65.911 39.186 −50.805 1.00 36.83 N ATOM 5034 CA VAL 630 66.073 39.385 −49.373 1.00 36.83 C ATOM 5035 CB VAL 630 64.839 40.094 −48.748 1.00 36.83 C ATOM 5036 CG1 VAL 630 64.903 40.003 −47.239 1.00 36.83 C ATOM 5037 CG2 VAL 630 64.781 41.560 −49.183 1.00 36.83 C ATOM 5038 C VAL 630 66.207 37.994 −48.757 1.00 36.83 C ATOM 5039 O VAL 630 67.049 37.769 −47.897 1.00 36.83 O ATOM 5040 N ALA 631 65.380 37.058 −49.211 1.00 36.83 N ATOM 5041 CA ALA 631 65.434 35.689 −48.709 1.00 36.83 C ATOM 5042 CB ALA 631 64.425 34.837 −49.434 1.00 36.83 C ATOM 5043 C ALA 631 66.832 35.082 −48.879 1.00 36.83 C ATOM 5044 O ALA 631 67.389 34.538 −47.935 1.00 36.83 O ATOM 5045 N ALA 632 67.382 35.172 −50.088 1.00 36.83 N ATOM 5046 CA ALA 632 68.711 34.634 −50.394 1.00 36.83 C ATOM 5047 CB ALA 632 68.997 34.772 −51.870 1.00 36.83 C ATOM 5048 C ALA 632 69.809 35.330 −49.577 1.00 36.83 C ATOM 5049 O ALA 632 70.685 34.678 −49.030 1.00 36.83 O ATOM 5050 N GLN 633 69.792 36.630 −49.568 1.00 36.83 N ATOM 5051 CA GLN 633 70.642 37.391 −48.733 1.00 36.83 C ATOM 5052 CB GLN 633 70.205 38.814 −48.829 1.00 36.83 C ATOM 5053 CG GLN 633 71.165 39.748 −48.320 1.00 36.83 C ATOM 5054 CD GLN 633 70.585 41.108 −48.181 1.00 36.83 C ATOM 5055 OE1 GLN 633 70.594 41.684 −47.108 1.00 36.83 O ATOM 5056 NE2 GLN 633 70.055 41.626 −49.264 1.00 36.83 N ATOM 5057 C GLN 633 70.679 36.940 −47.288 1.00 36.83 C ATOM 5058 O GLN 633 71.716 36.709 −46.749 1.00 36.83 O ATOM 5059 N TYR 634 69.538 36.866 −46.652 1.00 36.83 N ATOM 5060 CA TYR 634 69.493 36.476 −45.249 1.00 36.83 C ATOM 5061 CB TYR 634 68.097 36.654 −44.648 1.00 36.83 C ATOM 5062 CG TYR 634 68.113 36.399 −43.162 1.00 36.83 C ATOM 5063 CD1 TYR 634 68.865 37.207 −42.313 1.00 36.83 C ATOM 5064 CE1 TYR 634 68.944 36.949 −40.957 1.00 36.83 C ATOM 5065 CD2 TYR 634 67.434 35.319 −42.610 1.00 36.83 C ATOM 5066 CE2 TYR 634 67.505 35.046 −41.244 1.00 36.83 C ATOM 5067 CZ TYR 634 68.260 35.872 −40.426 1.00 36.83 C ATOM 5068 OH TYR 634 68.292 35.654 −39.071 1.00 36.83 O ATOM 5069 C TYR 634 69.965 35.056 −44.969 1.00 36.83 C ATOM 5070 O TYR 634 70.655 34.814 −43.973 1.00 36.83 O ATOM 5071 N LYS 635 69.585 34.119 −45.832 1.00 36.83 N ATOM 5072 CA LYS 635 69.992 32.731 −45.651 1.00 36.83 C ATOM 5073 CB LYS 635 69.456 31.854 −46.785 1.00 36.83 C ATOM 5074 CG LYS 635 69.633 30.350 −46.557 1.00 36.83 C ATOM 5075 CD LYS 635 69.194 29.516 −47.769 1.00 36.83 C ATOM 5076 CE LYS 635 69.311 27.993 −47.487 1.00 36.83 C ATOM 5077 NZ LYS 635 69.214 27.136 −48.714 1.00 36.83 N ATOM 5078 C LYS 635 71.513 32.645 −45.608 1.00 36.83 C ATOM 5079 O LYS 635 72.058 31.906 −44.798 1.00 36.83 O ATOM 5080 N GLU 636 72.202 33.400 −46.462 1.00 36.83 N ATOM 5081 CA GLU 636 73.670 33.373 −46.481 1.00 36.83 C ATOM 5082 CB GLU 636 74.228 34.093 −47.709 1.00 36.83 C ATOM 5083 CG GLU 636 75.446 33.404 −48.343 1.00 36.83 C ATOM 5084 CD GLU 636 76.687 33.336 −47.428 1.00 36.83 C ATOM 5085 OE1 GLU 636 77.662 32.618 −47.800 1.00 36.83 O ATOM 5086 OE2 GLU 636 76.702 33.997 −46.350 1.00 36.83 O ATOM 5087 C GLU 636 74.257 34.013 −45.225 1.00 36.83 C ATOM 5088 O GLU 636 75.225 33.507 −44.679 1.00 36.83 O ATOM 5089 N GLN 637 73.686 35.118 −44.794 1.00 36.83 N ATOM 5090 CA GLN 637 74.141 35.727 −43.578 1.00 36.83 C ATOM 5091 CB GLN 637 73.520 37.072 −43.349 1.00 36.83 C ATOM 5092 CG GLN 637 73.909 38.090 −44.339 1.00 36.83 C ATOM 5093 CD GLN 637 73.024 39.275 −44.297 1.00 36.83 C ATOM 5094 OE1 GLN 637 73.057 40.113 −45.170 1.00 36.83 O ATOM 5095 NE2 GLN 637 72.217 39.358 −43.281 1.00 36.83 N ATOM 5096 C GLN 637 73.965 34.841 −42.385 1.00 36.83 C ATOM 5097 O GLN 637 74.819 34.779 −41.557 1.00 36.83 O ATOM 5098 N LEU 638 72.845 34.160 −42.318 1.00 36.83 N ATOM 5099 CA LEU 638 72.562 33.250 −41.223 1.00 36.83 C ATOM 5100 CB LEU 638 71.113 32.755 −41.286 1.00 36.83 C ATOM 5101 CG LEU 638 70.690 31.751 −40.200 1.00 36.83 C ATOM 5102 CD1 LEU 638 71.058 32.273 −38.810 1.00 36.83 C ATOM 5103 CD2 LEU 638 69.185 31.498 −40.291 1.00 36.83 C ATOM 5104 C LEU 638 73.525 32.074 −41.305 1.00 36.83 C ATOM 5105 O LEU 638 73.979 31.568 −40.287 1.00 36.83 O ATOM 5106 N ALA 639 73.833 31.641 −42.525 1.00 36.83 N ATOM 5107 CA ALA 639 74.764 30.532 −42.721 1.00 36.83 C ATOM 5108 CB ALA 639 74.780 30.098 −44.188 1.00 36.83 C ATOM 5109 C ALA 639 76.169 30.952 −42.279 1.00 36.83 C ATOM 5110 O ALA 639 76.878 30.189 −41.631 1.00 36.83 O ATOM 5111 N SER 640 76.573 32.166 −42.628 1.00 36.83 N ATOM 5112 CA SER 640 77.890 32.633 −42.226 1.00 36.83 C ATOM 5113 CB SER 640 78.166 34.022 −42.803 1.00 36.83 C ATOM 5114 OG SER 640 79.316 34.594 −42.204 1.00 36.83 O ATOM 5115 C SER 640 77.977 32.683 −40.700 1.00 36.83 C ATOM 5116 O SER 640 78.975 32.249 −40.112 1.00 36.83 O ATOM 5117 N LEU 641 76.935 33.219 −40.062 1.00 36.83 N ATOM 5118 CA LEU 641 76.895 33.321 −38.604 1.00 36.83 C ATOM 5119 CB LEU 641 75.556 33.897 −38.125 1.00 36.83 C ATOM 5120 CG LEU 641 75.329 33.868 −36.604 1.00 36.83 C ATOM 5121 CD1 LEU 641 76.376 34.742 −35.921 1.00 36.83 C ATOM 5122 CD2 LEU 641 73.926 34.364 −36.257 1.00 36.83 C ATOM 5123 C LEU 641 77.090 31.961 −37.961 1.00 36.83 C ATOM 5124 O LEU 641 77.936 31.795 −37.082 1.00 36.83 O ATOM 5125 N MET 642 76.302 30.992 −38.411 1.00 36.83 N ATOM 5126 CA MET 642 76.368 29.644 −37.879 1.00 36.83 C ATOM 5127 CB MET 642 75.302 28.769 −38.538 1.00 36.83 C ATOM 5128 CG MET 642 73.887 29.276 −38.342 1.00 36.83 C ATOM 5129 SD MET 642 73.518 29.590 −36.615 1.00 36.83 S ATOM 5130 CE MET 642 73.696 27.919 −35.977 1.00 36.83 C ATOM 5131 C MET 642 77.752 29.041 −38.097 1.00 36.83 C ATOM 5132 O MET 642 78.256 28.287 −37.246 1.00 36.83 O ATOM 5133 N ALA 643 78.357 29.361 −39.242 1.00 36.83 N ATOM 5134 CA ALA 643 79.696 28.868 −39.556 1.00 36.83 C ATOM 5135 CB ALA 643 80.147 29.379 −40.926 1.00 36.83 C ATOM 5136 C ALA 643 80.637 29.368 −38.459 1.00 36.83 C ATOM 5137 O ALA 643 81.428 28.604 −37.904 1.00 36.83 O ATOM 5138 N THR 644 80.532 30.653 −38.136 1.00 36.83 N ATOM 5139 CA THR 644 81.362 31.233 −37.093 1.00 36.83 C ATOM 5140 CB THR 644 81.117 32.737 −36.995 1.00 36.83 C ATOM 5141 OG1 THR 644 81.648 33.369 −38.167 1.00 36.83 O ATOM 5142 CG2 THR 644 81.781 33.316 −35.754 1.00 36.83 C ATOM 5143 C THR 644 81.122 30.585 −35.723 1.00 36.83 C ATOM 5144 O THR 644 82.058 30.375 −34.945 1.00 36.83 O ATOM 5145 N LEU 645 79.868 30.250 −35.438 1.00 36.83 N ATOM 5146 CA LEU 645 79.544 29.637 −34.160 1.00 36.83 C ATOM 5147 CB LEU 645 78.026 29.587 −33.968 1.00 36.83 C ATOM 5148 CG LEU 645 77.365 30.967 −33.854 1.00 36.83 C ATOM 5149 CD1 LEU 645 75.856 30.854 −34.048 1.00 36.83 C ATOM 5150 CD2 LEU 645 77.698 31.573 −32.497 1.00 36.83 C ATOM 5151 C LEU 645 80.139 28.233 −34.042 1.00 36.83 C ATOM 5152 O LEU 645 80.523 27.804 −32.967 1.00 36.83 O ATOM 5153 N GLU 646 80.229 27.523 −35.154 1.00 36.83 N ATOM 5154 CA GLU 646 80.765 26.177 −35.100 1.00 36.83 C ATOM 5155 CB GLU 646 80.543 25.453 −36.430 1.00 36.83 C ATOM 5156 CG GLU 646 80.744 23.946 −36.332 1.00 36.83 C ATOM 5157 CD GLU 646 79.657 23.275 −35.495 1.00 36.83 C ATOM 5158 OE1 GLU 646 79.986 22.684 −34.439 1.00 36.83 O ATOM 5159 OE2 GLU 646 78.466 23.345 −35.897 1.00 36.83 O ATOM 5160 C GLU 646 82.253 26.202 −34.771 1.00 36.83 C ATOM 5161 O GLU 646 82.839 25.159 −34.526 1.00 36.83 O ATOM 5162 N THR 647 82.857 27.393 −34.753 1.00 36.83 N ATOM 5163 CA THR 647 84.280 27.510 −34.459 1.00 36.83 C ATOM 5164 CB THR 647 84.997 28.481 −35.440 1.00 36.83 C ATOM 5165 OG1 THR 647 84.859 29.833 −34.985 1.00 36.83 O ATOM 5166 CG2 THR 647 84.394 28.354 −36.836 1.00 36.83 C ATOM 5167 C THR 647 84.538 27.972 −33.035 1.00 36.83 C ATOM 5168 O THR 647 85.680 28.027 −32.594 1.00 36.83 O ATOM 5169 N THR 648 83.480 28.305 −32.308 1.00 36.83 N ATOM 5170 CA THR 648 83.647 28.738 −30.928 1.00 36.83 C ATOM 5171 CB THR 648 82.835 30.022 −30.609 1.00 36.83 C ATOM 5172 OG1 THR 648 81.436 29.712 −30.566 1.00 36.83 O ATOM 5173 CG2 THR 648 83.075 31.090 −31.663 1.00 36.83 C ATOM 5174 C THR 648 83.141 27.640 −30.022 1.00 36.83 C ATOM 5175 O THR 648 82.468 26.712 −30.478 1.00 36.83 O ATOM 5176 N ASN 649 83.493 27.732 −28.746 1.00 36.83 N ATOM 5177 CA ASN 649 83.024 26.792 −27.741 1.00 36.83 C ATOM 5178 CB ASN 649 84.056 26.597 −26.636 1.00 36.83 C ATOM 5179 CG ASN 649 83.548 25.704 −25.520 1.00 36.83 C ATOM 5180 OD1 ASN 649 83.184 24.555 −25.753 1.00 36.83 O ATOM 5181 ND2 ASN 649 83.529 26.225 −24.303 1.00 36.83 N ATOM 5182 C ASN 649 81.863 27.590 −27.197 1.00 36.83 C ATOM 5183 O ASN 649 82.065 28.692 −26.680 1.00 36.83 O ATOM 5184 N PRO 650 80.634 27.062 −27.331 1.00 36.83 N ATOM 5185 CD PRO 650 80.332 26.001 −28.314 1.00 36.83 C ATOM 5186 CA PRO 650 79.397 27.713 −26.873 1.00 36.83 C ATOM 5187 CB PRO 650 78.370 27.198 −27.878 1.00 36.83 C ATOM 5188 CG PRO 650 78.845 25.793 −28.132 1.00 36.83 C ATOM 5189 C PRO 650 78.885 27.591 −25.427 1.00 36.83 C ATOM 5190 O PRO 650 78.947 26.534 −24.803 1.00 36.83 O ATOM 5191 N HIS 651 78.355 28.694 −24.910 1.00 36.83 N ATOM 5192 CA HIS 651 77.771 28.724 −23.571 1.00 36.83 C ATOM 5193 CB HIS 651 78.491 29.731 −22.672 1.00 36.83 C ATOM 5194 CG HIS 651 79.940 29.418 −22.467 1.00 36.83 C ATOM 5195 CD2 HIS 651 80.549 28.569 −21.611 1.00 36.83 C ATOM 5196 ND1 HIS 651 80.935 29.937 −23.270 1.00 36.83 N ATOM 5197 CE1 HIS 651 82.094 29.415 −22.918 1.00 36.83 C ATOM 5198 NE2 HIS 651 81.889 28.581 −21.915 1.00 36.83 N ATOM 5199 C HIS 651 76.311 29.135 −23.763 1.00 36.83 C ATOM 5200 O HIS 651 76.016 30.173 −24.369 1.00 36.83 O ATOM 5201 N PHE 652 75.398 28.318 −23.255 1.00 36.83 N ATOM 5202 CA PHE 652 73.982 28.591 −23.424 1.00 36.83 C ATOM 5203 CB PHE 652 73.261 27.298 −23.795 1.00 36.83 C ATOM 5204 CG PHE 652 73.560 26.821 −25.180 1.00 36.83 C ATOM 5205 CD1 PHE 652 72.958 27.411 −26.269 1.00 36.83 C ATOM 5206 CD2 PHE 652 74.478 25.804 −25.396 1.00 36.83 C ATOM 5207 CE1 PHE 652 73.259 27.008 −27.555 1.00 36.83 C ATOM 5208 CE2 PHE 652 74.789 25.395 −26.684 1.00 36.83 C ATOM 5209 CZ PHE 652 74.173 26.003 −27.771 1.00 36.83 C ATOM 5210 C PHE 652 73.266 29.234 −22.253 1.00 36.83 C ATOM 5211 O PHE 652 73.401 28.793 −21.119 1.00 36.83 O ATOM 5212 N VAL 653 72.504 30.282 −22.554 1.00 36.83 N ATOM 5213 CA VAL 653 71.684 30.986 −21.576 1.00 36.83 C ATOM 5214 CB VAL 653 72.099 32.470 −21.435 1.00 36.83 C ATOM 5215 CG1 VAL 653 71.205 33.153 −20.418 1.00 36.83 C ATOM 5216 CG2 VAL 653 73.547 32.572 −20.987 1.00 36.83 C ATOM 5217 C VAL 653 70.218 30.931 −22.062 1.00 36.83 C ATOM 5218 O VAL 653 69.871 31.526 −23.085 1.00 36.83 O ATOM 5219 N ARG 654 69.366 30.203 −21.348 1.00 36.83 N ATOM 5220 CA ARG 654 67.954 30.106 −21.738 1.00 36.83 C ATOM 5221 CB ARG 654 67.434 28.667 −21.577 1.00 36.83 C ATOM 5222 CG ARG 654 68.425 27.546 −21.898 1.00 36.83 C ATOM 5223 CD ARG 654 69.069 27.687 −23.261 1.00 36.83 C ATOM 5224 NE ARG 654 68.124 27.696 −24.382 1.00 36.83 N ATOM 5225 CZ ARG 654 67.530 26.622 −24.900 1.00 36.83 C ATOM 5226 NH1 ARG 654 67.761 25.414 −24.405 1.00 36.83 N ATOM 5227 NH2 ARG 654 66.719 26.758 −25.943 1.00 36.83 N ATOM 5228 C ARG 654 67.077 31.062 −20.891 1.00 36.83 C ATOM 5229 O ARG 654 66.944 30.901 −19.677 1.00 36.83 O ATOM 5230 N CYS 655 66.513 32.073 −21.536 1.00 36.83 N ATOM 5231 CA CYS 655 65.649 33.012 −20.838 1.00 36.83 C ATOM 5232 CB CYS 655 65.739 34.408 −21.461 1.00 36.83 C ATOM 5233 SG CYS 655 67.373 35.187 −21.323 1.00 36.83 S ATOM 5234 C CYS 655 64.228 32.479 −20.940 1.00 36.83 C ATOM 5235 O CYS 655 63.822 31.973 −21.977 1.00 36.83 O ATOM 5236 N ILE 656 63.487 32.571 −19.850 1.00 36.83 N ATOM 5237 CA ILE 656 62.124 32.091 −19.828 1.00 36.83 C ATOM 5238 CB ILE 656 61.935 30.977 −18.790 1.00 36.83 C ATOM 5239 CG2 ILE 656 60.513 30.443 −18.864 1.00 36.83 C ATOM 5240 CG1 ILE 656 62.960 29.860 −19.013 1.00 36.83 C ATOM 5241 CD1 ILE 656 62.791 29.085 −20.308 1.00 36.83 C ATOM 5242 C ILE 656 61.243 33.257 −19.435 1.00 36.83 C ATOM 5243 O ILE 656 61.513 33.932 −18.437 1.00 36.83 O ATOM 5244 N ILE 657 60.205 33.508 −20.230 1.00 36.83 N ATOM 5245 CA ILE 657 59.281 34.592 −19.926 1.00 36.83 C ATOM 5246 CB ILE 657 58.584 35.118 −21.217 1.00 36.83 C ATOM 5247 CG2 ILE 657 57.409 34.228 −21.594 1.00 36.83 C ATOM 5248 CG1 ILE 657 58.148 36.564 −21.007 1.00 36.83 C ATOM 5249 CD1 ILE 657 57.657 37.241 −22.246 1.00 36.83 C ATOM 5250 C ILE 657 58.276 34.009 −18.930 1.00 36.83 C ATOM 5251 O ILE 657 57.715 32.944 −19.153 1.00 36.83 O ATOM 5252 N PRO 658 58.065 34.694 −17.799 1.00 36.83 N ATOM 5253 CD PRO 658 58.733 35.943 −17.398 1.00 36.83 C ATOM 5254 CA PRO 658 57.141 34.249 −16.749 1.00 36.83 C ATOM 5255 CB PRO 658 57.430 35.223 −15.609 1.00 36.83 C ATOM 5256 CG PRO 658 57.812 36.462 −16.320 1.00 36.83 C ATOM 5257 C PRO 658 55.669 34.206 −17.126 1.00 36.83 C ATOM 5258 O PRO 658 54.920 33.372 −16.618 1.00 36.83 O ATOM 5259 N ASN 659 55.256 35.103 −18.011 1.00 36.83 N ATOM 5260 CA ASN 659 53.867 35.160 −18.459 1.00 36.83 C ATOM 5261 CB ASN 659 52.997 35.798 −17.380 1.00 36.83 C ATOM 5262 CG ASN 659 53.541 37.126 −16.912 1.00 36.83 C ATOM 5263 OD1 ASN 659 53.585 38.101 −17.668 1.00 36.83 O ATOM 5264 ND2 ASN 659 53.974 37.172 −15.668 1.00 36.83 N ATOM 5265 C ASN 659 53.796 35.969 −19.740 1.00 36.83 C ATOM 5266 O ASN 659 54.820 36.312 −20.302 1.00 36.83 O ATOM 5267 N ASN 660 52.594 36.266 −20.212 1.00 36.83 N ATOM 5268 CA ASN 660 52.458 37.045 −21.439 1.00 36.83 C ATOM 5269 CB ASN 660 51.603 36.281 −22.464 1.00 36.83 C ATOM 5270 CG ASN 660 52.111 34.864 −22.716 1.00 36.83 C ATOM 5271 OD1 ASN 660 51.419 33.886 −22.433 1.00 36.83 O ATOM 5272 ND2 ASN 660 53.326 34.748 −23.243 1.00 36.83 N ATOM 5273 C ASN 660 51.855 38.430 −21.169 1.00 36.83 C ATOM 5274 O ASN 660 51.295 39.050 −22.063 1.00 36.83 O ATOM 5275 N LYS 661 51.976 38.909 −19.934 1.00 36.83 N ATOM 5276 CA LYS 661 51.449 40.224 −19.564 1.00 36.83 C ATOM 5277 CB LYS 661 50.451 40.096 −18.404 1.00 36.83 C ATOM 5278 CG LYS 661 48.995 39.952 −18.806 1.00 36.83 C ATOM 5279 CD LYS 661 48.514 38.512 −18.806 1.00 36.83 C ATOM 5280 CE LYS 661 48.345 37.966 −17.386 1.00 36.83 C ATOM 5281 NZ LYS 661 47.753 36.585 −17.382 1.00 36.83 N ATOM 5282 C LYS 661 52.553 41.216 −19.157 1.00 36.83 C ATOM 5283 O LYS 661 52.268 42.348 −18.779 1.00 36.83 O ATOM 5284 N GLN 662 53.809 40.795 −19.240 1.00 36.83 N ATOM 5285 CA GLN 662 54.919 41.654 −18.855 1.00 36.83 C ATOM 5286 CB GLN 662 55.024 42.865 −19.806 1.00 36.83 C ATOM 5287 CG GLN 662 55.774 42.538 −21.109 1.00 36.83 C ATOM 5288 CD GLN 662 55.814 43.686 −22.125 1.00 36.83 C ATOM 5289 OE1 GLN 662 54.868 43.893 −22.880 1.00 36.83 O ATOM 5290 NE2 GLN 662 56.928 44.432 −22.143 1.00 36.83 N ATOM 5291 C GLN 662 54.736 42.103 −17.411 1.00 36.83 C ATOM 5292 O GLN 662 54.988 43.250 −17.064 1.00 36.83 O ATOM 5293 N LEU 663 54.304 41.170 −16.569 1.00 36.83 N ATOM 5294 CA LEU 663 54.079 41.442 −15.155 1.00 36.83 C ATOM 5295 CB LEU 663 52.629 41.125 −14.776 1.00 36.83 C ATOM 5296 CG LEU 663 51.495 41.882 −15.466 1.00 36.83 C ATOM 5297 CD1 LEU 663 50.146 41.280 −15.052 1.00 36.83 C ATOM 5298 CD2 LEU 663 51.585 43.362 −15.108 1.00 36.83 C ATOM 5299 C LEU 663 55.004 40.636 −14.234 1.00 36.83 C ATOM 5300 O LEU 663 55.354 39.497 −14.524 1.00 36.83 O ATOM 5301 N PRO 664 55.403 41.238 −13.107 1.00 36.83 N ATOM 5302 CD PRO 664 55.249 42.683 −12.848 1.00 36.83 C ATOM 5303 CA PRO 664 56.277 40.628 −12.101 1.00 36.83 C ATOM 5304 CB PRO 664 56.859 41.838 −11.376 1.00 36.83 C ATOM 5305 CG PRO 664 55.748 42.816 −11.415 1.00 36.83 C ATOM 5306 C PRO 664 55.494 39.723 −11.158 1.00 36.83 C ATOM 5307 O PRO 664 54.269 39.787 −11.108 1.00 36.83 O ATOM 5308 N ALA 665 56.199 38.876 −10.420 1.00 36.83 N ATOM 5309 CA ALA 665 55.550 37.980 −9.459 1.00 36.83 C ATOM 5310 CB ALA 665 55.192 38.764 −8.200 1.00 36.83 C ATOM 5311 C ALA 665 54.296 37.268 −9.993 1.00 36.83 C ATOM 5312 O ALA 665 53.296 37.176 −9.294 1.00 36.83 O ATOM 5313 N LYS 666 54.349 36.770 −11.225 1.00 36.83 N ATOM 5314 CA LYS 666 53.214 36.075 −11.798 1.00 36.83 C ATOM 5315 CB LYS 666 52.312 37.057 −12.524 1.00 36.83 C ATOM 5316 CG LYS 666 50.917 36.528 −12.766 1.00 36.83 C ATOM 5317 CD LYS 666 50.018 37.598 −13.375 1.00 36.83 C ATOM 5318 CE LYS 666 48.603 37.054 −13.582 1.00 36.83 C ATOM 5319 NZ LYS 666 47.790 37.905 −14.500 1.00 36.83 N ATOM 5320 C LYS 666 53.686 34.974 −12.744 1.00 36.83 C ATOM 5321 O LYS 666 53.463 35.017 −13.953 1.00 36.83 O ATOM 5322 N LEU 667 54.335 33.978 −12.149 1.00 36.83 N ATOM 5323 CA LEU 667 54.892 32.828 −12.844 1.00 36.83 C ATOM 5324 CB LEU 667 55.888 32.125 −11.919 1.00 36.83 C ATOM 5325 CG LEU 667 56.791 31.066 −12.535 1.00 36.83 C ATOM 5326 CD1 LEU 667 57.767 31.749 −13.484 1.00 36.83 C ATOM 5327 CD2 LEU 667 57.517 30.312 −11.439 1.00 36.83 C ATOM 5328 C LEU 667 53.791 31.859 −13.226 1.00 36.83 C ATOM 5329 O LEU 667 53.402 31.042 −12.405 1.00 36.83 O ATOM 5330 N GLU 668 53.305 31.941 −14.466 1.00 36.83 N ATOM 5331 CA GLU 668 52.221 31.067 −14.948 1.00 36.83 C ATOM 5332 CB GLU 668 51.423 31.761 −16.057 1.00 36.83 C ATOM 5333 CG GLU 668 50.744 33.044 −15.606 1.00 36.83 C ATOM 5334 CD GLU 668 50.123 33.820 −16.761 1.00 36.83 C ATOM 5335 OE1 GLU 668 50.789 33.983 −17.811 1.00 36.83 O ATOM 5336 OE2 GLU 668 48.969 34.281 −16.615 1.00 36.83 O ATOM 5337 C GLU 668 52.784 29.749 −15.468 1.00 36.83 C ATOM 5338 O GLU 668 53.517 29.720 −16.457 1.00 36.83 O ATOM 5339 N ASP 669 52.419 28.661 −14.801 1.00 36.83 N ATOM 5340 CA ASP 669 52.930 27.346 −15.154 1.00 36.83 C ATOM 5341 CB ASP 669 52.400 26.313 −14.156 1.00 36.83 C ATOM 5342 CG ASP 669 50.913 26.417 −13.949 1.00 36.83 C ATOM 5343 OD1 ASP 669 50.187 26.470 −14.967 1.00 36.83 O ATOM 5344 OD2 ASP 669 50.470 26.438 −12.774 1.00 36.83 O ATOM 5345 C ASP 669 52.737 26.853 −16.599 1.00 36.83 C ATOM 5346 O ASP 669 53.645 26.269 −17.181 1.00 36.83 O ATOM 5347 N LYS 670 51.576 27.080 −17.190 1.00 36.83 N ATOM 5348 CA LYS 670 51.369 26.613 −18.561 1.00 36.83 C ATOM 5349 CB LYS 670 49.923 26.874 −18.984 1.00 36.83 C ATOM 5350 CG LYS 670 49.311 25.782 −19.843 1.00 36.83 C ATOM 5351 CD LYS 670 50.100 25.541 −21.126 1.00 36.83 C ATOM 5352 CE LYS 670 49.499 24.389 −21.910 1.00 36.83 C ATOM 5353 NZ LYS 670 49.198 23.231 −20.994 1.00 36.83 N ATOM 5354 C LYS 670 52.359 27.329 −19.514 1.00 36.83 C ATOM 5355 O LYS 670 52.942 26.710 −20.413 1.00 36.83 O ATOM 5356 N VAL 671 52.543 28.629 −19.304 1.00 36.83 N ATOM 5357 CA VAL 671 53.463 29.410 −20.121 1.00 36.83 C ATOM 5358 CB VAL 671 53.372 30.915 −19.790 1.00 36.83 C ATOM 5359 CG1 VAL 671 54.378 31.698 −20.632 1.00 36.83 C ATOM 5360 CG2 VAL 671 51.967 31.416 −20.048 1.00 36.83 C ATOM 5361 C VAL 671 54.919 28.966 −19.939 1.00 36.83 C ATOM 5362 O VAL 671 55.648 28.828 −20.910 1.00 36.83 O ATOM 5363 N VAL 672 55.326 28.733 −18.694 1.00 36.83 N ATOM 5364 CA VAL 672 56.696 28.317 −18.390 1.00 36.83 C ATOM 5365 CB VAL 672 56.985 28.418 −16.853 1.00 36.83 C ATOM 5366 CG1 VAL 672 58.328 27.817 −16.522 1.00 36.83 C ATOM 5367 CG2 VAL 672 56.964 29.881 −16.417 1.00 36.83 C ATOM 5368 C VAL 672 57.010 26.900 −18.877 1.00 36.83 C ATOM 5369 O VAL 672 58.064 26.659 −19.464 1.00 36.83 O ATOM 5370 N LEU 673 56.085 25.976 −18.625 1.00 36.83 N ATOM 5371 CA LEU 673 56.243 24.581 −19.021 1.00 36.83 C ATOM 5372 CB LEU 673 55.022 23.765 −18.554 1.00 36.83 C ATOM 5373 CG LEU 673 55.227 22.646 −17.523 1.00 36.83 C ATOM 5374 CD1 LEU 673 56.575 22.766 −16.821 1.00 36.83 C ATOM 5375 CD2 LEU 673 54.096 22.695 −16.494 1.00 36.83 C ATOM 5376 C LEU 673 56.447 24.453 −20.537 1.00 36.83 C ATOM 5377 O LEU 673 57.384 23.779 −20.976 1.00 36.83 O ATOM 5378 N ASP 674 55.591 25.102 −21.328 1.00 36.83 N ATOM 5379 CA ASP 674 55.718 25.072 −22.788 1.00 36.83 C ATOM 5380 CB ASP 674 54.823 26.118 −23.471 1.00 36.83 C ATOM 5381 CG ASP 674 53.357 25.737 −23.503 1.00 36.83 C ATOM 5382 OD1 ASP 674 53.034 24.564 −23.765 1.00 36.83 O ATOM 5383 OD2 ASP 674 52.522 26.641 −23.290 1.00 36.83 O ATOM 5384 C ASP 674 57.153 25.419 −23.165 1.00 36.83 C ATOM 5385 O ASP 674 57.738 24.793 −24.035 1.00 36.83 O ATOM 5386 N GLN 675 57.702 26.447 −22.529 1.00 36.83 N ATOM 5387 CA GLN 675 59.066 26.863 −22.824 1.00 36.83 C ATOM 5388 CB GLN 675 59.374 28.208 −22.154 1.00 36.83 C ATOM 5389 CG GLN 675 58.500 29.341 −22.646 1.00 36.83 C ATOM 5390 CD GLN 675 58.773 30.661 −21.932 1.00 36.83 C ATOM 5391 OE1 GLN 675 59.712 31.388 −22.273 1.00 36.83 O ATOM 5392 NE2 GLN 675 57.957 30.966 −20.929 1.00 36.83 N ATOM 5393 C GLN 675 60.069 25.800 −22.383 1.00 36.83 C ATOM 5394 O GLN 675 60.947 25.425 −23.146 1.00 36.83 O ATOM 5395 N LEU 676 59.922 25.297 −21.161 1.00 36.83 N ATOM 5396 CA LEU 676 60.840 24.276 −20.676 1.00 36.83 C ATOM 5397 CB LEU 676 60.472 23.826 −19.264 1.00 36.83 C ATOM 5398 CG LEU 676 60.548 24.915 −18.200 1.00 36.83 C ATOM 5399 CD1 LEU 676 60.348 24.269 −16.854 1.00 36.83 C ATOM 5400 CD2 LEU 676 61.872 25.659 −18.274 1.00 36.83 C ATOM 5401 C LEU 676 60.820 23.090 −21.618 1.00 36.83 C ATOM 5402 O LEU 676 61.867 22.524 −21.930 1.00 36.83 O ATOM 5403 N ARG 677 59.626 22.719 −22.076 1.00 36.83 N ATOM 5404 CA ARG 677 59.519 21.604 −22.998 1.00 36.83 C ATOM 5405 CB ARG 677 58.052 21.229 −23.250 1.00 36.83 C ATOM 5406 CG ARG 677 57.426 20.408 −22.116 1.00 36.83 C ATOM 5407 CD ARG 677 56.065 19.831 −22.489 1.00 36.83 C ATOM 5408 NE ARG 677 55.028 20.852 −22.620 1.00 36.83 N ATOM 5409 CZ ARG 677 54.283 21.318 −21.624 1.00 36.83 C ATOM 5410 NH1 ARG 677 54.436 20.857 −20.403 1.00 36.83 N ATOM 5411 NH2 ARG 677 53.391 22.266 −21.854 1.00 36.83 N ATOM 5412 C ARG 677 60.221 21.882 −24.324 1.00 36.83 C ATOM 5413 O ARG 677 61.215 21.232 −24.642 1.00 36.83 O ATOM 5414 N CYS 678 59.753 22.865 −25.086 1.00 36.83 N ATOM 5415 CA CYS 678 60.376 23.097 −26.377 1.00 36.83 C ATOM 5416 CB CYS 678 59.535 24.077 −27.205 1.00 36.83 C ATOM 5417 SG CYS 678 59.769 25.815 −26.898 1.00 36.83 S ATOM 5418 C CYS 678 61.857 23.506 −26.345 1.00 36.83 C ATOM 5419 O CYS 678 62.570 23.297 −27.325 1.00 36.83 O ATOM 5420 N ASN 679 62.330 24.056 −25.228 1.00 36.83 N ATOM 5421 CA ASN 679 63.746 24.440 −25.124 1.00 36.83 C ATOM 5422 CB ASN 679 63.992 25.401 −23.946 1.00 36.83 C ATOM 5423 CG ASN 679 63.562 26.832 −24.233 1.00 36.83 C ATOM 5424 OD1 ASN 679 63.771 27.716 −23.404 1.00 36.83 O ATOM 5425 ND2 ASN 679 62.969 27.068 −25.397 1.00 36.83 N ATOM 5426 C ASN 679 64.595 23.187 −24.895 1.00 36.83 C ATOM 5427 O ASN 679 65.814 23.202 −25.102 1.00 36.83 O ATOM 5428 N GLY 680 63.944 22.118 −24.446 1.00 36.83 N ATOM 5429 CA GLY 680 64.638 20.872 −24.172 1.00 36.83 C ATOM 5430 C GLY 680 65.510 20.972 −22.922 1.00 36.83 C ATOM 5431 O GLY 680 66.608 20.415 −22.878 1.00 36.83 O ATOM 5432 N VAL 681 65.022 21.688 −21.912 1.00 36.83 N ATOM 5433 CA VAL 681 65.753 21.872 −20.667 1.00 36.83 C ATOM 5434 CB VAL 681 65.070 22.918 −19.762 1.00 36.83 C ATOM 5435 CG1 VAL 681 65.643 22.859 −18.357 1.00 36.83 C ATOM 5436 CG2 VAL 681 65.278 24.294 −20.341 1.00 36.83 C ATOM 5437 C VAL 681 65.886 20.582 −19.886 1.00 36.83 C ATOM 5438 O VAL 681 66.974 20.246 −19.419 1.00 36.83 O ATOM 5439 N LEU 682 64.783 19.860 −19.745 1.00 36.83 N ATOM 5440 CA LEU 682 64.802 18.609 −19.013 1.00 36.83 C ATOM 5441 CB LEU 682 63.392 18.033 −18.877 1.00 36.83 C ATOM 5442 CG LEU 682 62.577 18.740 −17.795 1.00 36.83 C ATOM 5443 CD1 LEU 682 62.096 20.062 −18.322 1.00 36.83 C ATOM 5444 CD2 LEU 682 61.408 17.878 −17.373 1.00 36.83 C ATOM 5445 C LEU 682 65.736 17.586 −19.634 1.00 36.83 C ATOM 5446 O LEU 682 66.454 16.901 −18.911 1.00 36.83 O ATOM 5447 N GLU 683 65.736 17.486 −20.962 1.00 36.83 N ATOM 5448 CA GLU 683 66.622 16.546 −21.635 1.00 36.83 C ATOM 5449 CB GLU 683 66.277 16.414 −23.123 1.00 36.83 C ATOM 5450 CG GLU 683 64.900 15.823 −23.433 1.00 36.83 C ATOM 5451 CD GLU 683 63.805 16.877 −23.474 1.00 36.83 C ATOM 5452 OE1 GLU 683 62.659 16.531 −23.827 1.00 36.83 O ATOM 5453 OE2 GLU 683 64.086 18.053 −23.153 1.00 36.83 O ATOM 5454 C GLU 683 68.041 17.087 −21.482 1.00 36.83 C ATOM 5455 O GLU 683 69.014 16.331 −21.398 1.00 36.83 O ATOM 5456 N GLY 684 68.142 18.411 −21.441 1.00 36.83 N ATOM 5457 CA GLY 684 69.431 19.053 −21.275 1.00 36.83 C ATOM 5458 C GLY 684 70.026 18.691 −19.928 1.00 36.83 C ATOM 5459 O GLY 684 71.249 18.679 −19.771 1.00 36.83 O ATOM 5460 N ILE 685 69.164 18.383 −18.962 1.00 36.83 N ATOM 5461 CA ILE 685 69.616 18.008 −17.631 1.00 36.83 C ATOM 5462 CB ILE 685 68.553 18.287 −16.560 1.00 36.83 C ATOM 5463 CG2 ILE 685 69.123 17.976 −15.184 1.00 36.83 C ATOM 5464 CG1 ILE 685 68.101 19.744 −16.627 1.00 36.83 C ATOM 5465 CD1 ILE 685 66.844 20.011 −15.839 1.00 36.83 C ATOM 5466 C ILE 685 69.934 16.523 −17.586 1.00 36.83 C ATOM 5467 O ILE 685 70.933 16.117 −16.994 1.00 36.83 O ATOM 5468 N ARG 686 69.090 15.713 −18.218 1.00 36.83 N ATOM 5469 CA ARG 686 69.310 14.272 −18.233 1.00 36.83 C ATOM 5470 CB ARG 686 68.146 13.538 −18.921 1.00 36.83 C ATOM 5471 CG ARG 686 67.226 12.842 −17.921 1.00 36.83 C ATOM 5472 CD ARG 686 66.246 11.852 −18.570 1.00 36.83 C ATOM 5473 NE ARG 686 65.052 12.503 −19.108 1.00 36.83 N ATOM 5474 CZ ARG 686 64.129 13.118 −18.372 1.00 36.83 C ATOM 5475 NH1 ARG 686 64.248 13.171 −17.049 1.00 36.83 N ATOM 5476 NH2 ARG 686 63.089 13.691 −18.968 1.00 36.83 N ATOM 5477 C ARG 686 70.626 13.876 −18.894 1.00 36.83 C ATOM 5478 O ARG 686 71.334 13.002 −18.389 1.00 36.83 O ATOM 5479 N ILE 687 70.969 14.511 −20.008 1.00 36.83 N ATOM 5480 CA ILE 687 72.206 14.165 −20.696 1.00 36.83 C ATOM 5481 CB ILE 687 72.383 14.972 −22.010 1.00 36.83 C ATOM 5482 CG2 ILE 687 73.297 16.168 −21.803 1.00 36.83 C ATOM 5483 CG1 ILE 687 72.987 14.070 −23.082 1.00 36.83 C ATOM 5484 CD1 ILE 687 74.215 13.318 −22.632 1.00 36.83 C ATOM 5485 C ILE 687 73.360 14.436 −19.755 1.00 36.83 C ATOM 5486 O ILE 687 74.352 13.724 −19.758 1.00 36.83 O ATOM 5487 N THR 688 73.237 15.481 −18.947 1.00 36.83 N ATOM 5488 CA THR 688 74.289 15.779 −17.999 1.00 36.83 C ATOM 5489 CB THR 688 74.004 17.078 −17.211 1.00 36.83 C ATOM 5490 OG1 THR 688 74.188 18.221 −18.069 1.00 36.83 O ATOM 5491 CG2 THR 688 74.934 17.187 −16.014 1.00 36.83 C ATOM 5492 C THR 688 74.357 14.601 −17.033 1.00 36.83 C ATOM 5493 O THR 688 75.081 13.636 −17.272 1.00 36.83 O ATOM 5494 N ARG 689 73.574 14.660 −15.967 1.00 36.83 N ATOM 5495 CA ARG 689 73.573 13.610 −14.958 1.00 36.83 C ATOM 5496 CB ARG 689 72.199 13.523 −14.313 1.00 36.83 C ATOM 5497 CG ARG 689 71.740 14.837 −43.740 1.00 36.83 C ATOM 5498 CD ARG 689 70.245 14.996 −13.900 1.00 36.83 C ATOM 5499 NE ARG 689 69.492 14.136 −12.991 1.00 36.83 N ATOM 5500 CZ ARG 689 68.936 12.977 −13.328 1.00 36.83 C ATOM 5501 NH1 ARG 689 69.040 12.508 −14.569 1.00 36.83 N ATOM 5502 NH2 ARG 689 68.255 12.295 −12.418 1.00 36.83 N ATOM 5503 C ARG 689 73.965 12.238 −15.490 1.00 36.83 C ATOM 5504 O ARG 689 74.904 11.607 −14.985 1.00 36.83 O ATOM 5505 N LYS 690 73.254 11.792 −16.522 1.00 36.83 N ATOM 5506 CA LYS 690 73.483 10.488 −17.134 1.00 36.83 C ATOM 5507 CB LYS 690 72.231 10.098 −17.917 1.00 36.83 C ATOM 5508 CG LYS 690 72.480 9.293 −19.170 1.00 36.83 C ATOM 5509 CD LYS 690 71.198 9.134 −19.987 1.00 36.83 C ATOM 5510 CE LYS 690 70.114 8.360 −19.236 1.00 36.83 C ATOM 5511 NZ LYS 690 69.018 7.911 −20.163 1.00 36.83 N ATOM 5512 C LYS 690 74.720 10.415 −18.036 1.00 36.83 C ATOM 5513 O LYS 690 75.202 9.323 −18.358 1.00 36.83 O ATOM 5514 N GLY 691 75.249 11.571 −18.431 1.00 36.83 N ATOM 5515 CA GLY 691 76.403 11.577 −19.314 1.00 36.83 C ATOM 5516 C GLY 691 77.802 11.700 −18.719 1.00 36.83 C ATOM 5517 O GLY 691 78.009 11.793 −17.504 1.00 36.83 O ATOM 5518 N PHE 692 78.774 11.795 −19.619 1.00 36.83 N ATOM 5519 CA PHE 692 80.178 11.922 −19.254 1.00 36.83 C ATOM 5520 CB PHE 692 80.984 10.763 −19.851 1.00 36.83 C ATOM 5521 CG PHE 692 80.443 9.407 −19.475 1.00 36.83 C ATOM 5522 CD1 PHE 692 80.405 9.008 −18.146 1.00 36.83 C ATOM 5523 CD2 PHE 692 79.920 8.556 −20.448 1.00 36.83 C ATOM 5524 CE1 PHE 692 79.850 7.779 −17.780 1.00 36.83 C ATOM 5525 CE2 PHE 692 79.362 7.327 −20.099 1.00 36.83 C ATOM 5526 CZ PHE 692 79.326 6.941 −18.760 1.00 36.83 C ATOM 5527 C PHE 692 80.676 13.256 −19.793 1.00 36.83 C ATOM 5528 O PHE 692 81.208 13.347 −20.909 1.00 36.83 O ATOM 5529 N PRO 693 80.488 14.314 −19.004 1.00 36.83 N ATOM 5530 CD PRO 693 79.901 14.212 −17.655 1.00 36.83 C ATOM 5531 CA PRO 693 80.882 15.692 −19.308 1.00 36.83 C ATOM 5532 CB PRO 693 80.837 16.356 −17.938 1.00 36.83 C ATOM 5533 CG PRO 693 79.630 15.660 −17.300 1.00 36.83 C ATOM 5534 C PRO 693 82.259 15.826 −19.971 1.00 36.83 C ATOM 5535 O PRO 693 82.396 15.703 −21.200 1.00 36.83 O ATOM 5536 N ASN 694 83.274 16.085 −19.149 1.00 36.83 N ATOM 5537 CA ASN 694 84.643 16.261 −19.639 1.00 36.83 C ATOM 5538 CB ASN 694 85.507 16.942 −18.573 1.00 36.83 C ATOM 5539 CG ASN 694 84.778 18.083 −17.854 1.00 36.83 C ATOM 5540 OD1 ASN 694 85.355 18.762 −16.985 1.00 36.83 O ATOM 5541 ND2 ASN 694 83.499 18.295 −18.205 1.00 36.83 N ATOM 5542 C ASN 694 85.238 14.904 −19.997 1.00 36.83 C ATOM 5543 O ASN 694 84.722 13.860 −19.581 1.00 36.83 O ATOM 5544 N ARG 695 86.312 14.916 −20.779 1.00 36.83 N ATOM 5545 CA ARG 695 86.971 13.679 −21.190 1.00 36.83 C ATOM 5546 CB ARG 695 86.632 13.376 −22.644 1.00 36.83 C ATOM 5547 CG ARG 695 85.136 13.365 −22.955 1.00 36.83 C ATOM 5548 CD ARG 695 84.810 14.143 −24.234 1.00 36.83 C ATOM 5549 NE ARG 695 85.811 13.955 −25.288 1.00 36.83 N ATOM 5550 CZ ARG 695 86.988 14.583 −25.342 1.00 36.83 C ATOM 5551 NH1 ARG 695 87.331 15.460 −24.395 1.00 36.83 N ATOM 5552 NH2 ARG 695 87.826 14.335 −26.353 1.00 36.83 N ATOM 5553 C ARG 695 88.480 13.861 −21.038 1.00 36.83 C ATOM 5554 O ARG 695 89.258 13.422 −21.894 1.00 36.83 O ATOM 5555 N ILE 696 88.885 14.499 −19.937 1.00 36.83 N ATOM 5556 CA ILE 696 90.300 14.789 −19.672 1.00 36.83 C ATOM 5557 CB ILE 696 90.536 15.120 −18.181 1.00 36.83 C ATOM 5558 CG2 ILE 696 89.968 16.503 −17.866 1.00 36.83 C ATOM 5559 CG1 ILE 696 89.929 14.030 −17.297 1.00 36.83 C ATOM 5560 CD1 ILE 696 90.200 14.223 −15.817 1.00 36.83 C ATOM 5561 C ILE 696 91.304 13.721 −20.101 1.00 36.83 C ATOM 5562 O ILE 696 90.954 12.553 −20.345 1.00 36.83 O ATOM 5563 N ILE 697 92.564 14.134 −20.182 1.00 36.83 N ATOM 5564 CA ILE 697 93.633 13.236 −20.599 1.00 36.83 C ATOM 5565 CB ILE 697 93.968 13.485 −22.099 1.00 36.83 C ATOM 5566 CG2 ILE 697 92.949 12.776 −22.990 1.00 36.83 C ATOM 5567 CG1 ILE 697 93.924 14.993 −22.387 1.00 36.83 C ATOM 5568 CD1 ILE 697 94.406 15.392 −23.776 1.00 36.83 C ATOM 5569 C ILE 697 94.914 13.349 −19.749 1.00 36.83 C ATOM 5570 O ILE 697 95.415 14.449 −19.486 1.00 36.83 O ATOM 5571 N TYR 698 95.430 12.203 −19.316 0.00 36.83 N ATOM 5572 CA TYR 698 96.661 12.150 −18.529 0.00 36.83 C ATOM 5573 CB TYR 698 97.865 12.237 −19.472 1.00 36.83 C ATOM 5574 CG TYR 698 97.490 11.994 −20.921 1.00 36.83 C ATOM 5575 CD1 TYR 698 96.936 10.770 −21.326 1.00 36.83 C ATOM 5576 CE1 TYR 698 96.508 10.562 −22.647 1.00 36.83 C ATOM 5577 CD2 TYR 698 97.624 13.010 −21.872 1.00 36.83 C ATOM 5578 CE2 TYR 698 97.211 12.823 −23.194 1.00 36.83 C ATOM 5579 CZ TYR 698 96.646 11.598 −23.576 1.00 36.83 C ATOM 5580 OH TYR 698 96.188 11.431 −24.862 1.00 36.83 O ATOM 5581 C TYR 698 96.741 13.265 −17.489 0.00 36.83 C ATOM 5582 O TYR 698 97.788 13.892 −17.319 0.00 36.83 O ATOM 5583 N ALA 699 95.634 13.510 −16.796 0.00 36.83 N ATOM 5584 CA ALA 699 95.588 14.551 −15.776 0.00 36.83 C ATOM 5585 CB ALA 699 94.161 15.064 −15.620 0.00 36.83 C ATOM 5586 C ALA 699 96.107 14.032 −14.440 0.00 36.83 C ATOM 5587 O ALA 699 95.811 12.905 −14.044 0.00 36.83 O ATOM 5588 N ASP 700 96.882 14.862 −13.748 0.00 36.83 N ATOM 5589 CA ASP 700 97.443 14.489 −12.455 0.00 36.83 C ATOM 5590 CB ASP 700 98.754 13.722 −12.651 0.00 36.83 C ATOM 5591 CG ASP 700 99.342 13.226 −11.343 0.00 36.83 C ATOM 5592 OD1 ASP 700 100.427 12.607 −11.376 0.00 36.83 O ATOM 5593 OD2 ASP 700 98.720 13.450 −10.283 0.00 36.83 O ATOM 5594 C ASP 700 97.692 15.725 −11.596 0.00 36.83 C ATOM 5595 O ASP 700 96.856 16.099 −10.774 0.00 36.83 O ATOM 5596 N PHE 701 98.846 16.356 −11.793 0.00 36.83 N ATOM 5597 CA PHE 701 99.205 17.550 −11.036 0.00 36.83 C ATOM 5598 CB PHE 701 99.676 17.159 −9.632 0.00 36.83 C ATOM 5599 CG PHE 701 100.007 18.333 −8.753 0.00 36.83 C ATOM 5600 CD1 PHE 701 99.041 19.288 −8.453 0.00 36.83 C ATOM 5601 CD2 PHE 701 101.284 18.483 −8.224 0.00 36.83 C ATOM 5602 CE1 PHE 701 99.343 20.377 −7.638 0.00 36.83 C ATOM 5603 CE2 PHE 701 101.597 19.568 −7.407 0.00 36.83 C ATOM 5604 CZ PHE 701 100.623 20.517 −7.114 0.00 36.83 C ATOM 5605 C PHE 701 100.302 18.335 −11.748 0.00 36.83 C ATOM 5606 O PHE 701 101.185 17.754 −12.379 0.00 36.83 O ATOM 5607 N VAL 702 100.240 19.659 −11.641 0.00 36.83 N ATOM 5608 CA VAL 702 101.224 20.528 −12.275 0.00 36.83 C ATOM 5609 CB VAL 702 100.799 22.010 −12.182 0.00 36.83 C ATOM 5610 CG1 VAL 702 99.478 22.217 −12.904 0.00 36.83 C ATOM 5611 CG2 VAL 702 100.678 22.426 −10.725 0.00 36.83 C ATOM 5612 C VAL 702 102.600 20.375 −11.635 0.00 36.83 C ATOM 5613 O VAL 702 102.714 20.009 −10.466 0.00 36.83 O ATOM 5614 N LYS 703 103.641 20.658 −12.411 0.00 36.83 N ATOM 5615 CA LYS 703 105.012 20.554 −11.925 0.00 36.83 C ATOM 5616 CB LYS 703 105.980 20.425 −13.104 0.00 36.83 C ATOM 5617 CG LYS 703 107.441 20.294 −12.701 0.00 36.83 C ATOM 5618 CD LYS 703 108.350 20.191 −13.918 0.00 36.83 C ATOM 5619 CE LYS 703 108.046 18.948 −14.741 0.00 36.83 C ATOM 5620 NZ LYS 703 108.930 18.843 −15.934 0.00 36.83 N ATOM 5621 C LYS 703 105.382 21.774 −11.089 0.00 36.83 C ATOM 5622 O LYS 703 105.230 22.912 −11.534 0.00 36.83 O ATOM 5623 N ARG 704 105.867 21.531 −9.876 0.00 36.83 N ATOM 5624 CA ARG 704 106.258 22.610 −8.977 0.00 36.83 C ATOM 5625 CB ARG 704 105.028 23.160 −8.248 0.00 36.83 C ATOM 5626 CG ARG 704 105.315 24.316 −7.298 0.00 36.83 C ATOM 5627 CD ARG 704 105.772 25.568 −8.037 0.00 36.83 C ATOM 5628 NE ARG 704 107.056 25.385 −8.708 0.00 36.83 N ATOM 5629 CZ ARG 704 107.669 26.326 −9.419 0.00 36.83 C ATOM 5630 NH1 ARG 704 108.836 26.070 −9.994 0.00 36.83 N ATOM 5631 NH2 ARG 704 107.117 27.524 −9.555 0.00 36.83 N ATOM 5632 C ARG 704 107.286 22.129 −7.958 0.00 36.83 C ATOM 5633 O ARG 704 108.447 22.335 −7.995 0.00 36.83 O ATOM 5634 N TYR 705 106.850 21.262 −7.049 0.00 36.83 N ATOM 5635 CA TYR 705 107.730 20.725 −6.018 0.00 36.83 C ATOM 5636 CB TYR 705 106.905 20.141 −4.867 0.00 36.83 C ATOM 5637 CG TYR 705 106.076 21.161 −4.118 0.00 36.83 C ATOM 5638 CD1 TYR 705 105.056 21.867 −4.756 0.00 36.83 C ATOM 5639 CE1 TYR 705 104.291 22.807 −4.069 0.00 36.83 C ATOM 5640 CD2 TYR 705 106.312 21.422 −2.768 0.00 36.83 C ATOM 5641 CE2 TYR 705 105.553 22.360 −2.072 0.00 36.83 C ATOM 5642 CZ TYR 705 104.545 23.048 −2.728 0.00 36.83 C ATOM 5643 OH TYR 705 103.793 23.976 −2.045 0.00 36.83 O ATOM 5644 C TYR 705 108.650 19.649 −6.584 0.00 36.83 C ATOM 5645 O TYR 705 108.602 19.342 −7.776 0.00 36.83 O ATOM 5646 N TYR 706 109.485 19.080 −5.722 0.00 36.83 N ATOM 5647 CA TYR 706 110.419 18.037 −6.130 0.00 36.83 C ATOM 5648 CB TYR 706 111.859 18.490 −5.866 0.00 36.83 C ATOM 5649 CG TYR 706 112.101 19.027 −4.471 0.00 36.83 C ATOM 5650 CD1 TYR 706 111.972 18.206 −3.351 0.00 36.83 C ATOM 5651 CE1 TYR 706 112.193 18.699 −2.067 0.00 36.83 C ATOM 5652 CD2 TYR 706 112.459 20.360 −4.271 0.00 36.83 C ATOM 5653 CE2 TYR 706 112.683 20.863 −2.991 0.00 36.83 C ATOM 5654 CZ TYR 706 112.548 20.027 −1.895 0.00 36.83 C ATOM 5655 OH TYR 706 112.767 20.519 −0.628 0.00 36.83 O ATOM 5656 C TYR 706 110.142 16.721 −5.409 0.00 36.83 C ATOM 5657 O TYR 706 109.028 16.481 −4.944 0.00 36.83 O ATOM 5658 N LEU 707 111.161 15.872 −5.322 0.00 36.83 N ATOM 5659 CA LEU 707 111.032 14.578 −4.663 0.00 36.83 C ATOM 5660 CB LEU 707 112.378 13.847 −4.671 0.00 36.83 C ATOM 5661 CG LEU 707 112.414 12.458 −4.028 0.00 36.83 C ATOM 5662 CD1 LEU 707 111.442 11.531 −4.743 0.00 36.83 C ATOM 5663 CD2 LEU 707 113.827 11.903 −4.096 0.00 36.83 C ATOM 5664 C LEU 707 110.539 14.727 −3.227 0.00 36.83 C ATOM 5665 O LEU 707 111.275 15.180 −2.351 0.00 36.83 O ATOM 5666 N LEU 708 109.288 14.341 −2.996 0.00 36.83 N ATOM 5667 CA LEU 708 108.687 14.424 −1.669 0.00 36.83 C ATOM 5668 CB LEU 708 107.943 15.753 −1.508 0.00 36.83 C ATOM 5669 CG LEU 708 108.791 17.028 −1.532 0.00 36.83 C ATOM 5670 CD1 LEU 708 107.884 18.247 −1.480 0.00 36.83 C ATOM 5671 CD2 LEU 708 109.753 17.025 −0.354 0.00 36.83 C ATOM 5672 C LEU 708 107.724 13.266 −1.435 0.00 36.83 C ATOM 5673 O LEU 708 108.057 12.298 −0.752 0.00 36.83 O ATOM 5674 N ALA 709 106.528 13.373 −2.007 0.00 36.83 N ATOM 5675 CA ALA 709 105.514 12.337 −1.862 0.00 36.83 C ATOM 5676 CB ALA 709 104.214 12.785 −2.519 0.00 36.83 C ATOM 5677 C ALA 709 105.990 11.027 −2.484 0.00 36.83 C ATOM 5678 O ALA 709 106.711 11.029 −3.482 0.00 36.83 O ATOM 5679 N PRO 710 105.591 9.888 −1.895 0.00 36.83 N ATOM 5680 CD PRO 710 104.782 9.776 −0.668 0.00 36.83 C ATOM 5681 CA PRO 710 105.972 8.560 −2.386 0.00 36.83 C ATOM 5682 CB PRO 710 105.157 7.624 −1.500 0.00 36.83 C ATOM 5683 CG PRO 710 105.095 8.371 −0.208 0.00 36.83 C ATOM 5684 C PRO 710 105.667 8.366 −3.869 0.00 36.83 C ATOM 5685 O PRO 710 106.202 7.460 −4.508 0.00 36.83 O ATOM 5686 N ASN 711 104.803 9.220 −4.409 1.00 36.83 N ATOM 5687 CA ASN 711 104.424 9.140 −5.818 1.00 36.83 C ATOM 5688 CB ASN 711 102.915 8.911 −5.942 0.00 36.83 C ATOM 5689 CG ASN 711 102.103 10.012 −5.290 0.00 36.83 C ATOM 5690 OD1 ASN 711 102.209 10.247 −4.086 0.00 36.83 O ATOM 5691 ND2 ASN 711 101.286 10.694 −6.083 0.00 36.83 N ATOM 5692 C ASN 711 104.819 10.401 −6.603 1.00 36.83 C ATOM 5693 O ASN 711 104.584 11.532 −6.157 1.00 36.83 O ATOM 5694 N VAL 712 105.433 10.197 −7.764 0.00 36.83 N ATOM 5695 CA VAL 712 105.842 11.302 −8.624 0.00 36.83 C ATOM 5696 CB VAL 712 107.335 11.655 −8.412 0.00 36.83 C ATOM 5697 CG1 VAL 712 107.674 12.951 −9.134 0.00 36.83 C ATOM 5698 CG2 VAL 712 107.637 11.784 −6.927 0.00 36.83 C ATOM 5699 C VAL 712 105.623 10.921 −10.092 0.00 36.83 C ATOM 5700 O VAL 712 106.477 11.168 −10.943 0.00 36.83 O ATOM 5701 N PRO 713 104.468 10.305 −10.407 1.00 36.83 N ATOM 5702 CD PRO 713 103.476 9.717 −9.484 1.00 36.83 C ATOM 5703 CA PRO 713 104.187 9.906 −11.791 1.00 36.83 C ATOM 5704 CB PRO 713 103.040 8.901 −11.638 1.00 36.83 C ATOM 5705 CG PRO 713 102.315 9.397 −10.407 1.00 36.83 C ATOM 5706 C PRO 713 103.834 11.054 −12.727 1.00 36.83 C ATOM 5707 O PRO 713 102.647 11.356 −12.953 1.00 36.83 O ATOM 5708 N ARG 714 104.872 11.679 −13.282 1.00 36.83 N ATOM 5709 CA ARG 714 104.705 12.803 −14.198 1.00 36.83 C ATOM 5710 CB ARG 714 105.870 13.786 −14.035 0.00 36.83 C ATOM 5711 CG ARG 714 105.755 15.074 −14.847 0.00 36.83 C ATOM 5712 CD ARG 714 106.078 14.857 −16.319 0.00 36.83 C ATOM 5713 NE ARG 714 106.052 16.107 −17.075 0.00 36.83 N ATOM 5714 CZ ARG 714 106.335 16.203 −18.370 0.00 36.83 C ATOM 5715 NH1 ARG 714 106.287 17.382 −18.976 0.00 36.83 N ATOM 5716 NH2 ARG 714 106.668 15.121 −19.061 0.00 36.83 N ATOM 5717 C ARG 714 104.651 12.272 −15.624 1.00 36.83 C ATOM 5718 O ARG 714 103.649 12.441 −16.329 1.00 36.83 O ATOM 5719 N ASP 715 105.737 11.631 −16.044 1.00 36.83 N ATOM 5720 CA ASP 715 105.818 11.066 −17.383 1.00 36.83 C ATOM 5721 CB ASP 715 107.103 11.525 −18.081 0.00 36.83 C ATOM 5722 CG ASP 715 108.357 11.128 −17.323 0.00 36.83 C ATOM 5723 OD1 ASP 715 108.631 9.914 −17.210 0.00 36.83 O ATOM 5724 OD2 ASP 715 109.070 12.032 −16.839 0.00 36.83 O ATOM 5725 C ASP 715 105.822 9.562 −17.207 1.00 36.83 C ATOM 5726 O ASP 715 106.467 9.047 −16.296 1.00 36.83 O ATOM 5727 N ALA 716 105.095 8.853 −18.065 1.00 36.83 N ATOM 5728 CA ALA 716 105.029 7.400 −17.963 1.00 36.83 C ATOM 5729 CB ALA 716 103.788 6.988 −17.160 1.00 36.83 C ATOM 5730 C ALA 716 105.004 6.769 −19.350 1.00 36.83 C ATOM 5731 O ALA 716 105.312 7.427 −20.350 1.00 36.83 O ATOM 5732 N GLU 717 104.657 5.487 −19.408 1.00 36.83 N ATOM 5733 CA GLU 717 104.591 4.766 −20.682 1.00 36.83 C ATOM 5734 CB GLU 717 105.377 3.456 −20.595 0.00 36.83 C ATOM 5735 CG GLU 717 105.384 2.646 −21.882 0.00 36.83 C ATOM 5736 CD GLU 717 106.179 1.360 −21.758 0.00 36.83 C ATOM 5737 OE1 GLU 717 107.391 1.436 −21.467 0.00 36.83 O ATOM 5738 OE2 GLU 717 105.593 0.275 −21.952 0.00 36.83 O ATOM 5739 C GLU 717 103.125 4.474 −20.954 1.00 36.83 C ATOM 5740 O GLU 717 102.706 4.324 −22.105 1.00 36.83 O ATOM 5741 N ASP 718 102.354 4.405 −19.871 1.00 36.83 N ATOM 5742 CA ASP 718 100.919 4.141 −19.938 1.00 36.83 C ATOM 5743 CB ASP 718 100.647 2.705 −19.490 1.00 36.83 C ATOM 5744 CG ASP 718 99.238 2.261 −19.789 1.00 36.83 C ATOM 5745 OD1 ASP 718 98.903 2.133 −20.995 1.00 36.83 O ATOM 5746 OD2 ASP 718 98.474 2.045 −18.819 1.00 36.83 O ATOM 5747 C ASP 718 100.221 5.135 −18.992 1.00 36.83 C ATOM 5748 O ASP 718 100.255 4.977 −17.761 1.00 36.83 O ATOM 5749 N SER 719 99.606 6.159 −19.575 0.00 36.83 N ATOM 5750 CA SER 719 98.922 7.198 −18.813 0.00 36.83 C ATOM 5751 CB SER 719 98.737 8.439 −19.687 0.00 36.83 C ATOM 5752 OG SER 719 98.019 8.120 −20.867 0.00 36.83 O ATOM 5753 C SER 719 97.570 6.771 −18.251 0.00 36.83 C ATOM 5754 O SER 719 97.080 7.358 −17.286 0.00 36.83 O ATOM 5755 N GLN 720 96.968 5.755 −18.860 1.00 36.83 N ATOM 5756 CA GLN 720 95.669 5.251 −18.417 1.00 36.83 C ATOM 5757 CB GLN 720 95.133 4.230 −19.424 0.00 36.83 C ATOM 5758 CG GLN 720 95.127 4.712 −20.868 0.00 36.83 C ATOM 5759 CD GLN 720 94.223 5.909 −21.089 0.00 36.83 C ATOM 5760 OE1 GLN 720 94.423 6.971 −20.500 0.00 36.83 O ATOM 5761 NE2 GLN 720 93.220 5.742 −21.943 0.00 36.83 N ATOM 5762 C GLN 720 95.813 4.587 −17.047 1.00 36.83 C ATOM 5763 O GLN 720 95.024 3.708 −16.675 1.00 36.83 O ATOM 5764 N LYS 721 96.826 5.008 −16.291 1.00 36.83 N ATOM 5765 CA LYS 721 97.053 4.436 −14.964 1.00 36.83 C ATOM 5766 CB LYS 721 98.114 3.336 −15.055 1.00 36.83 C ATOM 5767 CG LYS 721 97.706 2.190 −15.992 1.00 36.83 C ATOM 5768 CD LYS 721 96.349 1.582 −15.576 1.00 36.83 C ATOM 5769 CE LYS 721 96.479 0.552 −14.457 1.00 36.83 C ATOM 5770 NZ LYS 721 97.127 −0.704 −14.975 1.00 36.83 N ATOM 5771 C LYS 721 97.445 5.490 −13.927 1.00 36.83 C ATOM 5772 O LYS 721 97.531 5.204 −12.721 1.00 36.83 O ATOM 5773 N ALA 722 97.664 6.713 −14.398 1.00 36.83 N ATOM 5774 CA ALA 722 98.028 7.822 −13.519 1.00 36.83 C ATOM 5775 CB ALA 722 98.015 9.142 −14.321 1.00 36.83 C ATOM 5776 C ALA 722 97.078 7.932 −12.319 1.00 36.83 C ATOM 5777 O ALA 722 97.337 8.690 −11.369 1.00 36.83 O ATOM 5778 N THR 723 95.971 7.190 −12.362 1.00 36.83 N ATOM 5779 CA THR 723 94.994 7.231 −11.268 1.00 36.83 C ATOM 5780 CB THR 723 93.604 7.666 −11.782 0.00 36.83 C ATOM 5781 OG1 THR 723 92.673 7.681 −10.693 0.00 36.83 O ATOM 5782 CG2 THR 723 93.107 6.707 −12.853 0.00 36.83 C ATOM 5783 C THR 723 94.853 5.876 −10.573 1.00 36.83 C ATOM 5784 O THR 723 94.391 5.803 −9.416 1.00 36.83 O ATOM 5785 N ASP 724 95.254 4.815 −11.279 1.00 36.83 N ATOM 5786 CA ASP 724 95.175 3.454 −10.751 1.00 36.83 C ATOM 5787 CB ASP 724 95.080 2.445 −11.910 1.00 36.83 C ATOM 5788 CG ASP 724 93.661 2.315 −12.465 1.00 36.83 C ATOM 5789 OD1 ASP 724 93.507 2.088 −13.693 1.00 36.83 O ATOM 5790 OD2 ASP 724 92.692 2.430 −11.672 1.00 36.83 O ATOM 5791 C ASP 724 96.375 3.127 −9.859 1.00 36.83 C ATOM 5792 O ASP 724 96.660 1.949 −9.575 1.00 36.83 O ATOM 5793 N ALA 725 97.071 4.168 −9.414 0.00 36.83 N ATOM 5794 CA ALA 725 98.232 4.002 −8.549 0.00 36.83 C ATOM 5795 CB ALA 725 99.105 5.248 −8.600 0.00 36.83 C ATOM 5796 C ALA 725 97.770 3.740 −7.120 0.00 36.83 C ATOM 5797 O ALA 725 97.994 2.660 −6.573 0.00 36.83 O ATOM 5798 N VAL 726 97.125 4.737 −6.521 1.00 36.83 N ATOM 5799 CA VAL 726 96.621 4.615 −5.159 1.00 36.83 C ATOM 5800 CB VAL 726 97.548 5.339 −4.159 0.00 36.83 C ATOM 5801 CG1 VAL 726 98.935 4.720 −4.195 0.00 36.83 C ATOM 5802 CG2 VAL 726 97.619 6.822 −4.492 0.00 36.83 C ATOM 5803 C VAL 726 95.211 5.200 −5.033 1.00 36.83 C ATOM 5804 O VAL 726 94.817 5.647 −3.954 1.00 36.83 O ATOM 5805 N LEU 727 94.455 5.214 −6.132 1.00 36.83 N ATOM 5806 CA LEU 727 93.092 5.744 −6.099 1.00 36.83 C ATOM 5807 CB LEU 727 92.360 5.416 −7.402 0.00 36.83 C ATOM 5808 CG LEU 727 90.882 5.806 −7.494 0.00 36.83 C ATOM 5809 CD1 LEU 727 90.733 7.311 −7.345 0.00 36.83 C ATOM 5810 CD2 LEU 727 90.317 5.344 −8.828 0.00 36.83 C ATOM 5811 C LEU 727 92.412 5.037 −4.939 1.00 36.83 C ATOM 5812 O LEU 727 91.992 5.669 −3.945 1.00 36.83 O ATOM 5813 N LYS 728 92.339 3.711 −5.064 1.00 36.83 N ATOM 5814 CA LYS 728 91.743 2.868 −4.036 1.00 36.83 C ATOM 5815 CB LYS 728 91.505 1.457 −4.583 0.00 36.83 C ATOM 5816 CG LYS 728 92.756 0.781 −5.126 0.00 36.83 C ATOM 5817 CD LYS 728 92.463 −0.631 −5.603 0.00 36.83 C ATOM 5818 CE LYS 728 93.715 −1.299 −6.149 0.00 36.83 C ATOM 5819 NZ LYS 728 94.791 −1.392 −5.123 0.00 36.83 N ATOM 5820 C LYS 728 92.700 2.814 −2.847 1.00 36.83 C ATOM 5821 O LYS 728 93.085 1.723 −2.381 1.00 36.83 O ATOM 5822 N HIS 729 93.092 3.993 −2.365 1.00 36.83 N ATOM 5823 CA HIS 729 94.002 4.082 −1.229 1.00 36.83 C ATOM 5824 CB HIS 729 95.190 4.986 −1.565 1.00 36.83 C ATOM 5825 CG HIS 729 96.418 4.699 −0.755 1.00 36.83 C ATOM 5826 CD2 HIS 729 96.583 4.024 0.410 1.00 36.83 C ATOM 5827 ND1 HIS 729 97.674 5.123 −1.138 1.00 36.83 N ATOM 5828 CE1 HIS 729 98.560 4.719 −0.241 1.00 36.83 C ATOM 5829 NE2 HIS 729 97.925 4.053 0.708 1.00 36.83 N ATOM 5830 C HIS 729 93.247 4.636 −0.034 1.00 36.83 C ATOM 5831 O HIS 729 93.780 4.701 1.086 1.00 36.83 O ATOM 5832 N LEU 730 91.997 5.020 −0.285 1.00 36.83 N ATOM 5833 CA LEU 730 91.111 5.565 0.747 1.00 36.83 C ATOM 5834 CB LEU 730 90.688 6.990 0.381 0.00 36.83 C ATOM 5835 CG LEU 730 91.806 8.014 0.165 0.00 36.83 C ATOM 5836 CD1 LEU 730 91.206 9.338 −0.282 0.00 36.83 C ATOM 5837 CD2 LEU 730 92.600 8.190 1.449 0.00 36.83 C ATOM 5838 C LEU 730 89.865 4.667 0.856 1.00 36.83 C ATOM 5839 O LEU 730 88.945 4.936 1.643 1.00 36.83 O ATOM 5840 N ASN 731 89.852 3.602 0.058 0.00 36.83 N ATOM 5841 CA ASN 731 88.747 2.647 0.032 0.00 36.83 C ATOM 5842 CB ASN 731 88.338 2.260 1.457 0.00 36.83 C ATOM 5843 CG ASN 731 89.477 1.639 2.241 0.00 36.83 C ATOM 5844 OD1 ASN 731 90.016 0.601 1.858 0.00 36.83 O ATOM 5845 ND2 ASN 731 89.848 2.273 3.347 0.00 36.83 N ATOM 5846 C ASN 731 87.537 3.194 −0.722 0.00 36.83 C ATOM 5847 O ASN 731 86.433 2.659 −0.612 0.00 36.83 O ATOM 5848 N ILE 732 87.751 4.261 −1.486 0.00 36.83 N ATOM 5849 CA ILE 732 86.681 4.872 −2.271 0.00 36.83 C ATOM 5850 CB ILE 732 87.052 6.307 −2.713 0.00 36.83 C ATOM 5851 CG2 ILE 732 85.897 6.923 −3.489 0.00 36.83 C ATOM 5852 CG1 ILE 732 87.393 7.167 −1.494 0.00 36.83 C ATOM 5853 CD1 ILE 732 87.867 8.575 −1.845 1.00 36.83 C ATOM 5854 C ILE 732 86.470 4.030 −3.526 0.00 36.83 C ATOM 5855 O ILE 732 87.439 3.615 −4.162 0.00 36.83 O ATOM 5856 N ASP 733 85.215 3.775 −3.889 1.00 36.83 N ATOM 5857 CA ASP 733 84.953 2.979 −5.086 1.00 36.83 C ATOM 5858 CB ASP 733 84.290 1.656 −4.689 1.00 36.83 C ATOM 5859 CG ASP 733 83.558 1.745 −3.365 1.00 36.83 C ATOM 5860 OD1 ASP 733 84.218 1.602 −2.306 1.00 36.83 O ATOM 5861 OD2 ASP 733 82.326 1.974 −3.391 1.00 36.83 O ATOM 5862 C ASP 733 84.146 3.682 −6.210 1.00 36.83 C ATOM 5863 O ASP 733 82.895 3.717 −6.204 1.00 36.83 O ATOM 5864 N PRO 734 84.865 4.250 −7.196 1.00 36.83 N ATOM 5865 CD PRO 734 86.304 4.571 −7.059 1.00 36.83 C ATOM 5866 CA PRO 734 84.280 4.959 −8.345 1.00 36.83 C ATOM 5867 CB PRO 734 85.354 5.990 −8.691 1.00 36.83 C ATOM 5868 CG PRO 734 86.631 5.228 −8.403 1.00 36.83 C ATOM 5869 C PRO 734 83.892 4.128 −9.583 1.00 36.83 C ATOM 5870 O PRO 734 84.765 3.614 −10.302 1.00 36.83 O ATOM 5871 N GLU 735 82.584 4.018 −9.829 1.00 36.83 N ATOM 5872 CA GLU 735 82.059 3.313 −11.011 1.00 36.83 C ATOM 5873 CB GLU 735 81.027 2.251 −10.611 1.00 36.83 C ATOM 5874 CG GLU 735 80.699 1.261 −11.737 1.00 36.83 C ATOM 5875 CD GLU 735 79.670 0.228 −11.321 0.00 36.83 C ATOM 5876 OE1 GLU 735 79.936 −0.525 −10.361 0.00 36.83 O ATOM 5877 OE2 GLU 735 78.596 0.169 −11.955 0.00 36.83 O ATOM 5878 C GLU 735 81.404 4.394 −11.895 1.00 36.83 C ATOM 5879 O GLU 735 80.649 4.116 −12.847 1.00 36.83 O ATOM 5880 N GLN 736 81.712 5.644 −11.554 1.00 36.83 N ATOM 5881 CA GLN 736 81.217 6.787 −12.297 1.00 36.83 C ATOM 5882 CB GLN 736 81.407 8.063 −11.474 1.00 36.83 C ATOM 5883 CG GLN 736 82.876 8.446 −11.317 1.00 36.83 C ATOM 5884 CD GLN 736 83.258 9.639 −12.167 1.00 36.83 C ATOM 5885 OE1 GLN 736 83.086 10.792 −11.744 1.00 36.83 O ATOM 5886 NE2 GLN 736 83.766 9.380 −13.379 1.00 36.83 N ATOM 5887 C GLN 736 82.023 6.886 −13.602 1.00 36.83 C ATOM 5888 O GLN 736 81.460 7.080 −14.683 1.00 36.83 O ATOM 5889 N TYR 737 83.338 6.741 −13.521 1.00 36.83 N ATOM 5890 CA TYR 737 84.147 6.853 −14.732 1.00 36.83 C ATOM 5891 CB TYR 737 85.628 7.071 −14.367 1.00 36.83 C ATOM 5892 CG TYR 737 86.369 5.881 −13.764 1.00 36.83 C ATOM 5893 CD1 TYR 737 86.487 4.671 −14.456 1.00 36.83 C ATOM 5894 CE1 TYR 737 87.251 3.603 −13.940 1.00 36.83 C ATOM 5895 CD2 TYR 737 87.025 6.001 −12.533 1.00 36.83 C ATOM 5896 CE2 TYR 737 87.798 4.941 −12.001 1.00 36.83 C ATOM 5897 CZ TYR 737 87.907 3.748 −12.713 1.00 36.83 C ATOM 5898 OH TYR 737 88.680 2.716 −12.201 1.00 36.83 O ATOM 5899 C TYR 737 84.016 5.661 −15.664 1.00 36.83 C ATOM 5900 O TYR 737 83.383 4.666 −15.318 1.00 36.83 O ATOM 5901 N ARG 738 84.615 5.766 −16.851 1.00 36.83 N ATOM 5902 CA ARG 738 84.596 4.669 −17.815 1.00 36.83 C ATOM 5903 CB ARG 738 83.554 4.906 −18.902 1.00 36.83 C ATOM 5904 CG ARG 738 82.802 3.654 −19.302 1.00 36.83 C ATOM 5905 CD ARG 738 81.325 3.863 −19.038 1.00 36.83 C ATOM 5906 NE ARG 738 81.065 4.232 −17.647 1.00 36.83 N ATOM 5907 CZ ARG 738 80.643 3.373 −16.725 1.00 36.83 C ATOM 5908 NH1 ARG 738 80.428 3.780 −15.477 1.00 36.83 N ATOM 5909 NH2 ARG 738 80.429 2.103 −17.058 1.00 36.83 N ATOM 5910 C ARG 738 85.972 4.555 −18.463 1.00 36.83 C ATOM 5911 O ARG 738 86.987 4.954 −17.874 1.00 36.83 O ATOM 5912 N PHE 739 86.028 4.012 −19.675 1.00 36.83 N ATOM 5913 CA PHE 739 87.326 3.894 −20.325 1.00 36.83 C ATOM 5914 CB PHE 739 87.527 2.491 −20.906 1.00 36.83 C ATOM 5915 CG PHE 739 88.862 1.891 −20.555 1.00 36.83 C ATOM 5916 CD1 PHE 739 90.025 2.657 −20.658 1.00 36.83 C ATOM 5917 CD2 PHE 739 88.962 0.569 −20.120 1.00 36.83 C ATOM 5918 CE1 PHE 739 91.282 2.116 −20.330 1.00 36.83 C ATOM 5919 CE2 PHE 739 90.202 0.016 −19.791 1.00 36.83 C ATOM 5920 CZ PHE 739 91.369 0.792 −19.896 1.00 36.83 C ATOM 5921 C PHE 739 87.528 4.933 −21.410 1.00 36.83 C ATOM 5922 O PHE 739 87.320 6.138 −21.173 1.00 36.83 O ATOM 5923 N GLY 740 87.942 4.467 −22.590 1.00 36.83 N ATOM 5924 CA GLY 740 88.187 5.351 −23.716 1.00 36.83 C ATOM 5925 C GLY 740 89.333 4.862 −24.590 1.00 36.83 C ATOM 5926 O GLY 740 90.517 5.020 −24.238 1.00 36.83 O ATOM 5927 N ILE 741 88.985 4.275 −25.736 1.00 36.83 N ATOM 5928 CA ILE 741 89.970 3.748 −26.671 1.00 36.83 C ATOM 5929 CB ILE 741 89.364 3.537 −28.069 1.00 36.83 C ATOM 5930 CG2 ILE 741 88.987 4.866 −28.648 1.00 36.83 C ATOM 5931 CG1 ILE 741 90.380 2.854 −29.006 1.00 36.83 C ATOM 5932 CD1 ILE 741 90.830 1.433 −28.578 1.00 36.83 C ATOM 5933 C ILE 741 91.134 4.717 −26.794 1.00 36.83 C ATOM 5934 O ILE 741 92.244 4.327 −27.182 1.00 36.83 O ATOM 5935 N THR 742 90.874 5.983 −26.466 1.00 36.83 N ATOM 5936 CA THR 742 91.902 7.016 −26.535 1.00 36.83 C ATOM 5937 CB THR 742 91.929 7.675 −27.904 1.00 36.83 C ATOM 5938 OG1 THR 742 91.041 6.968 −28.772 1.00 36.83 O ATOM 5939 CG2 THR 742 93.345 7.664 −28.488 1.00 36.83 C ATOM 5940 C THR 742 91.671 8.125 −25.525 1.00 36.83 C ATOM 5941 O THR 742 92.400 9.125 −25.540 1.00 36.83 O ATOM 5942 N LYS 743 90.667 7.976 −24.660 1.00 36.83 N ATOM 5943 CA LYS 743 90.395 9.025 −23.679 1.00 36.83 C ATOM 5944 CB LYS 743 89.452 10.067 −24.301 1.00 36.83 C ATOM 5945 CG LYS 743 89.892 10.510 −25.682 1.00 36.83 C ATOM 5946 CD LYS 743 88.790 10.304 −26.703 1.00 36.83 C ATOM 5947 CE LYS 743 87.855 11.524 −26.758 1.00 36.83 C ATOM 5948 NZ LYS 743 87.274 11.866 −25.412 1.00 36.83 N ATOM 5949 C LYS 743 89.797 8.472 −22.389 1.00 36.83 C ATOM 5950 O LYS 743 89.410 7.303 −22.337 1.00 36.83 O ATOM 5951 N ILE 744 89.690 9.317 −21.364 1.00 36.83 N ATOM 5952 CA ILE 744 89.145 8.878 −20.078 1.00 36.83 C ATOM 5953 CB ILE 744 90.311 8.761 −19.023 1.00 36.83 C ATOM 5954 CG2 ILE 744 90.852 10.135 −18.658 1.00 36.83 C ATOM 5955 CG1 ILE 744 89.833 7.977 −17.809 1.00 36.83 C ATOM 5956 CD1 ILE 744 89.283 6.611 −18.192 1.00 36.83 C ATOM 5957 C ILE 744 87.968 9.731 −19.516 1.00 36.83 C ATOM 5958 O ILE 744 88.151 10.614 −18.676 1.00 36.83 O ATOM 5959 N PHE 745 86.750 9.426 −19.964 1.00 36.83 N ATOM 5960 CA PHE 745 85.545 10.155 −19.538 1.00 36.83 C ATOM 5961 CB PHE 745 84.322 9.655 −20.325 1.00 36.83 C ATOM 5962 CG PHE 745 84.467 9.739 −21.820 1.00 36.83 C ATOM 5963 CD1 PHE 745 85.435 8.990 −22.486 1.00 36.83 C ATOM 5964 CD2 PHE 745 83.618 10.558 −22.566 1.00 36.83 C ATOM 5965 CE1 PHE 745 85.563 9.053 −23.883 1.00 36.83 C ATOM 5966 CE2 PHE 745 83.729 10.634 −23.962 1.00 36.83 C ATOM 5967 CZ PHE 745 84.705 9.881 −24.624 1.00 36.83 C ATOM 5968 C PHE 745 85.212 10.065 −18.040 1.00 36.83 C ATOM 5969 O PHE 745 85.008 8.976 −17.503 1.00 36.83 O ATOM 5970 N PHE 746 85.125 11.207 −17.365 1.00 36.83 N ATOM 5971 CA PHE 746 84.763 11.192 −15.949 1.00 36.83 C ATOM 5972 CB PHE 746 85.947 11.648 −15.081 0.00 36.83 C ATOM 5973 CG PHE 746 86.257 13.114 −15.182 0.00 36.83 C ATOM 5974 CD1 PHE 746 86.639 13.681 −16.391 0.00 36.83 C ATOM 5975 CD2 PHE 746 86.168 13.930 −14.058 0.00 36.83 C ATOM 5976 CE1 PHE 746 86.929 15.039 −16.480 0.00 36.83 C ATOM 5977 CE2 PHE 746 86.456 15.290 −14.137 0.00 36.83 C ATOM 5978 CZ PHE 746 86.837 15.845 −15.351 0.00 36.83 C ATOM 5979 C PHE 746 83.510 12.036 −15.636 1.00 36.83 C ATOM 5980 O PHE 746 83.552 13.280 −15.626 1.00 36.83 O ATOM 5981 N ARG 747 82.400 11.343 −15.382 1.00 36.83 N ATOM 5982 CA ARG 747 81.119 11.976 −15.051 1.00 36.83 C ATOM 5983 CB ARG 747 80.205 10.986 −14.315 1.00 36.83 C ATOM 5984 CG ARG 747 79.847 9.702 −15.048 1.00 36.83 C ATOM 5985 CD ARG 747 79.175 8.729 −14.087 1.00 36.83 C ATOM 5986 NE ARG 747 78.613 7.569 −14.784 1.00 36.83 N ATOM 5987 CZ ARG 747 77.340 7.469 −15.151 1.00 36.83 C ATOM 5988 NH1 ARG 747 76.901 6.388 −15.788 1.00 36.83 N ATOM 5989 NH2 ARG 747 76.497 8.449 −14.859 1.00 36.83 N ATOM 5990 C ARG 747 81.272 13.201 −14.142 1.00 36.83 C ATOM 5991 O ARG 747 82.395 13.609 −13.780 1.00 36.83 O ATOM 5992 N ALA 748 80.125 13.764 −13.761 1.00 36.83 N ATOM 5993 CA ALA 748 80.087 14.904 −12.852 1.00 36.83 C ATOM 5994 CB ALA 748 79.111 15.967 −13.351 1.00 36.83 C ATOM 5995 C ALA 748 79.621 14362 −11.504 1.00 36.83 C ATOM 5996 O ALA 748 79.651 13.146 −11.278 1.00 36.83 O ATOM 5997 N GLY 749 79.183 15.257 −10.623 0.00 36.83 N ATOM 5998 CA GLY 749 78.716 14.839 −9.314 0.00 36.83 C ATOM 5999 C GLY 749 78.141 15.981 −8.498 0.00 36.83 C ATOM 6000 O GLY 749 78.584 17.124 −8.618 0.00 36.83 O ATOM 6001 N GLN 750 77.149 15.672 −7.668 0.00 36.83 N ATOM 6002 CA GLN 750 76.511 16.676 −6.823 0.00 36.83 C ATOM 6003 CB GLN 750 75.204 16.122 −6.245 0.00 36.83 C ATOM 6004 CG GLN 750 75.364 14.825 −5.465 0.00 36.83 C ATOM 6005 CD GLN 750 74.060 14.347 −4.858 0.00 36.83 C ATOM 6006 OE1 GLN 750 73.441 15.048 −4.058 0.00 36.83 O ATOM 6007 NE2 GLN 750 73.636 13.146 −5.235 0.00 36.83 N ATOM 6008 C GLN 750 77.448 17.090 −5.690 0.00 36.83 C ATOM 6009 O GLN 750 78.610 17.420 −5.930 0.00 36.83 O ATOM 6010 N LEU 751 76.939 17.077 −4.462 0.00 36.83 N ATOM 6011 CA LEU 751 77.738 17.443 −3.298 0.00 36.83 C ATOM 6012 CB LEU 751 76.985 17.102 −2.010 0.00 36.83 C ATOM 6013 CG LEU 751 75.639 17.798 −1.791 0.00 36.83 C ATOM 6014 CD1 LEU 751 75.000 17.282 −0.512 0.00 36.83 C ATOM 6015 CD2 LEU 751 75.843 19.303 −1.720 0.00 36.83 C ATOM 6016 C LEU 751 79.062 16.691 −3.333 0.00 36.83 C ATOM 6017 O LEU 751 79.094 15.490 −3.601 0.00 36.83 O ATOM 6018 N ALA 752 80.153 17.400 −3.064 1.00 36.83 N ATOM 6019 CA ALA 752 81.472 16.786 −3.083 1.00 36.83 C ATOM 6020 CB ALA 752 82.140 17.017 −4.451 1.00 36.83 C ATOM 6021 C ALA 752 82.371 17.314 −1.975 1.00 36.83 C ATOM 6022 O ALA 752 82.282 18.490 −1.584 1.00 36.83 O ATOM 6023 N ARG 753 83.244 16.432 −1.481 1.00 36.83 N ATOM 6024 CA ARG 753 84.184 16.773 −0.417 1.00 36.83 C ATOM 6025 CB ARG 753 84.453 15.548 0.455 1.00 36.83 C ATOM 6026 CG ARG 753 83.298 15.112 1.334 1.00 36.83 C ATOM 6027 CD ARG 753 83.638 13.758 1.949 1.00 36.83 C ATOM 6028 NE ARG 753 85.085 13.545 1.983 1.00 36.83 N ATOM 6029 CZ ARG 753 85.675 12.457 2.480 1.00 36.83 C ATOM 6030 NH1 ARG 753 87.004 12.351 2.464 1.00 36.83 N ATOM 6031 NH2 ARG 753 84.943 11.478 3.001 1.00 36.83 N ATOM 6032 C ARG 753 85.512 17.262 −0.990 1.00 36.83 C ATOM 6033 O ARG 753 85.867 18.445 −0.872 1.00 36.83 O ATOM 6034 N ILE 754 86.245 16.329 −1.598 1.00 36.83 N ATOM 6035 CA ILE 754 87.546 16.612 −2.196 1.00 36.83 C ATOM 6036 CB ILE 754 88.680 16.359 −1.165 1.00 36.83 C ATOM 6037 CG2 ILE 754 90.054 16.667 −1.793 1.00 36.83 C ATOM 6038 CG1 ILE 754 88.426 17.224 0.084 1.00 36.83 C ATOM 6039 CD1 ILE 754 89.580 17.269 1.102 1.00 36.83 C ATOM 6040 C ILE 754 87.709 15.715 −3.427 1.00 36.83 C ATOM 6041 O ILE 754 88.655 14.924 −3.536 1.00 36.83 O ATOM 6042 N LEU 755 86.765 15.857 −4.358 1.00 36.83 N ATOM 6043 CA LEU 755 86.745 15.070 −5.589 1.00 36.83 C ATOM 6044 CB LEU 755 85.429 14.276 −5.690 1.00 36.83 C ATOM 6045 CG LEU 755 85.338 13.226 −6.812 1.00 36.83 C ATOM 6046 CD1 LEU 755 86.490 12.241 −6.666 1.00 36.83 C ATOM 6047 CD2 LEU 755 83.999 12.489 −6.756 1.00 36.83 C ATOM 6048 C LEU 755 86.881 15.987 −6.795 1.00 36.83 C ATOM 6049 O LEU 755 87.724 15.672 −7.677 1.00 36.83 O ATOM 6050 OXT LEU 755 86.136 17.003 −6.843 1.00 36.83 O ATOM 6051 C1 h79 A 1 71.267 45.220 −46.141 1.00 20.00 C ATOM 6052 C2 h79 A 1 70.883 45.620 −44.891 1.00 20.00 C ATOM 6053 C3 h79 A 1 69.931 46.575 −44.752 1.00 20.00 C ATOM 6054 C4 h79 A 1 69.391 47.159 −45.868 1.00 20.00 C ATOM 6055 C5 h79 A 1 69.737 46.806 −47.157 1.00 20.00 C ATOM 6056 C6 h79 A 1 70.702 45.794 −47.316 1.00 20.00 C ATOM 6057 N7 h79 A 1 68.454 48.110 −45.957 1.00 20.00 N ATOM 6058 C8 h79 A 1 68.181 48.370 −47.229 1.00 20.00 C ATOM 6059 C9 h79 A 1 68.966 47.596 −48.040 1.00 20.00 C ATOM 6060 C10 h79 A 1 67.298 49.263 −47.706 1.00 20.00 C ATOM 6061 C11 h79 A 1 67.126 49.458 −49.066 1.00 20.00 C ATOM 6062 C12 h79 A 1 67.869 48.703 −49.934 1.00 20.00 C ATOM 6063 C13 h79 A 1 68.775 47.778 −49.443 1.00 20.00 C ATOM 6064 BR14 h79 A 1 72.589 43.876 −46.053 1.00 20.00 BR ATOM 6065 BR15 h79 A 1 69.597 46.982 −50.933 1.00 20.00 BR ATOM 6066 BR16 h79 A 1 67.656 48.831 −51.824 1.00 20.00 BR ATOM 6067 O17 h79 A 1 66.641 49.933 −46.741 1.00 20.00 O ATOM 6068 C31 AMV B 1001 64.294 42.627 −16.924 1.00 23.77 C ATOM 6069 N30 AMV B 1001 64.160 43.518 −15.948 1.00 27.47 N ATOM 6070 C29 AMV B 1001 64.981 43.511 −14.934 1.00 27.85 C ATOM 6071 N28 AMV B 1001 65.949 42.628 −14.841 1.00 25.39 N ATOM 6072 C26 AMV B 1001 66.130 41.693 −15.761 1.00 23.46 C ATOM 6073 C25 AMV B 1001 65.289 41.676 −16.847 1.00 22.61 C ATOM 6074 N27 AMV B 1001 67.111 40.811 −15.598 1.00 30.29 N ATOM 6075 N24 AMV B 1001 65.187 40.913 −17.912 1.00 22.91 N ATOM 6076 N22 AMV B 1001 63.625 42.421 −18.025 1.00 22.13 N ATOM 6077 C23 AMV B 1001 64.179 41.389 −18.618 1.00 22.95 C ATOM 6078 C21 AMV B 1001 62.457 43.201 −18.468 1.00 20.51 C ATOM 6079 C19 AMV B 1001 62.793 44.586 −18.958 1.00 23.23 C ATOM 6080 C17 AMV B 1001 62.732 44.475 −20.449 1.00 19.65 C ATOM 6081 C15 AMV B 1001 61.687 43.430 −20.651 1.00 15.03 C ATOM 6082 O16 AMV B 1001 61.727 42.613 −19.489 1.00 17.90 O ATOM 6083 O20 AMV B 1001 61.748 45.411 −18.554 1.00 36.85 O ATOM 6084 O18 AMV B 1001 62.476 45.678 −21.141 1.00 17.93 O ATOM 6085 C14 AMV B 1001 62.026 42.628 −21.900 1.00 9.23 C ATOM 6086 O13 AMV B 1001 63.360 42.127 −21.939 1.00 3.48 O ATOM 6087 P9 AMV B 1001 64.171 41.989 −23.234 1.00 0.00 P ATOM 6088 O10 AMV B 1001 65.456 41.569 −22.814 1.00 11.17 O ATOM 6089 O11 AMV B 1001 64.071 43.229 −23.891 1.00 0.00 O ATOM 6090 O12 AMV B 1001 63.500 40.823 −24.038 1.00 2.48 O ATOM 6091 P5 AMV B 1001 64.037 40.125 −25.340 1.00 7.43 P ATOM 6092 O8 AMV B 1001 62.819 40.326 −26.253 1.00 10.35 O ATOM 6093 V AMV B 1001 62.699 40.575 −28.314 1.00 125.83 V ATOM 6094 O7 AMV B 1001 64.146 38.708 −25.071 1.00 7.92 O ATOM 6095 O6 AMV B 1001 65.163 40.854 −25.852 1.00 24.12 O ATOM 6096 O3 AMV B 1001 60.734 41.058 −28.117 1.00 4.63 O ATOM 6097 O4 AMV B 1001 63.047 38.687 −28.804 1.00 11.34 O ATOM 6098 O2 AMV B 1001 64.344 41.814 −28.476 1.00 34.78 O ATOM 6099 O HOH D 1 64.005 31.246 −11.042 1.00 20.00 O ATOM 6100 O HOH D 2 61.848 19.608 −7.480 1.00 20.00 O ATOM 6101 O HOH D 3 51.066 20.323 −39.703 1.00 20.00 O ATOM 6102 O HOH D 4 76.392 25.736 −21.665 1.00 20.00 O ATOM 6103 O HOH D 5 46.568 22.041 −36.992 1.00 20.00 O ATOM 6104 O HOH D 6 48.121 20.249 −45.121 1.00 20.00 O ATOM 6105 O HOH D 7 34.232 16.102 −18.843 1.00 20.00 O ATOM 6106 O HOH D 8 51.489 57.460 −45.078 1.00 20.00 O ATOM 6107 O HOH D 9 58.579 20.778 −34.702 1.00 20.00 O ATOM 6108 O HOH D 10 68.981 42.818 −30.924 1.00 20.00 O ATOM 6109 O HOH D 11 64.810 30.043 −23.999 1.00 20.00 O ATOM 6110 O HOH D 12 53.422 41.050 −39.507 1.00 20.00 O ATOM 6111 O HOH D 13 46.960 24.197 −9.261 1.00 20.00 O ATOM 6112 O HOH D 14 68.532 35.540 −55.172 1.00 20.00 O ATOM 6113 O HOH D 15 63.944 47.903 −57.966 1.00 20.00 O ATOM 6114 O HOH D 16 62.779 62.495 −60.984 1.00 20.00 O ATOM 6115 O HOH D 17 60.747 18.227 −44.121 1.00 20.00 O ATOM 6116 O HOH D 18 95.077 8.387 −9.147 1.00 20.00 O ATOM 6117 O HOH D 19 61.506 19.570 −37.091 1.00 20.00 O ATOM 6118 O HOH D 20 46.809 34.554 −59.432 1.00 20.00 O ATOM 6119 O HOH D 21 56.334 49.520 −50.105 1.00 20.00 O ATOM 6120 O HOH D 22 51.485 23.526 −11.441 1.00 20.00 O ATOM 6121 O HOH D 23 51.702 38.943 −45.251 1.00 20.00 O ATOM 6122 O HOH D 24 59.228 61.588 −65.704 1.00 20.00 O ATOM 6123 O HOH D 25 57.712 20.837 −26.885 1.00 20.00 O ATOM 6124 O HOH D 26 54.582 3.922 1.495 1.00 20.00 O ATOM 6125 O HOH D 27 81.793 47.309 −17.007 1.00 20.00 O ATOM 6126 O HOH D 28 71.251 29.816 −43.556 1.00 20.00 O ATOM 6127 O HOH D 29 71.679 46.460 −10.067 1.00 20.00 O ATOM 6128 O HOH D 30 76.961 47.578 −44.179 1.00 20.00 O ATOM 6129 O HOH D 31 64.772 45.315 −22.799 1.00 20.00 O ATOM 6130 O HOH D 32 77.609 42.323 −1.630 1.00 20.00 O ATOM 6131 O HOH D 33 104.548 8.329 −15.304 1.00 20.00 O ATOM 6132 O HOH D 34 67.658 65.929 −55.857 1.00 20.00 O ATOM 6133 O HOH D 35 65.394 36.084 −18.556 1.00 20.00 O ATOM 6134 O HOH D 36 84.303 16.454 −16.357 1.00 20.00 O ATOM 6135 O HOH D 37 76.097 46.951 −21.236 1.00 20.00 O ATOM 6136 O HOH D 38 48.202 13.138 −12.488 1.00 20.00 O ATOM 6137 O HOH D 39 59.799 16.594 −34.215 1.00 20.00 O ATOM 6138 O HOH D 40 59.370 20.849 −52.882 1.00 20.00 O ATOM 6139 O HOH D 41 77.997 30.456 −10.585 1.00 20.00 O ATOM 6140 O HOH D 42 57.700 38.863 −59.284 1.00 20.00 O ATOM 6141 O HOH D 43 67.268 44.382 −12.739 1.00 20.00 O ATOM 6142 O HOH D 44 51.926 51.503 −24.166 1.00 20.00 O ATOM 6143 O HOH D 45 49.257 35.288 −40.043 1.00 20.00 O ATOM 6144 O HOH D 46 62.693 54.814 −61.844 1.00 20.00 O ATOM 6145 O HOH D 47 52.220 11.904 −10.701 1.00 20.00 O ATOM 6146 O HOH D 48 54.083 45.841 −24.932 1.00 20.00 O ATOM 6147 O HOH D 49 57.444 29.332 −60.105 1.00 20.00 O ATOM 6148 O HOH D 50 56.133 36.885 −13.283 1.00 20.00 O ATOM 6149 O HOH D 51 66.258 38.392 −17.330 1.00 20.00 O ATOM 6150 O HOH D 52 52.174 54.130 −66.229 1.00 20.00 O ATOM 6151 O HOH D 53 61.083 47.734 −10.678 1.00 20.00 O ATOM 6152 O HOH D 54 64.531 13.236 6.232 1.00 20.00 O ATOM 6153 O HOH D 55 60.293 52.743 −55.571 1.00 20.00 O ATOM 6154 O HOH D 56 52.108 43.526 −46.142 1.00 20.00 O ATOM 6155 O HOH D 57 60.063 19.385 −3.511 1.00 20.00 O ATOM 6156 O HOH D 58 75.563 45.451 −40.060 1.00 20.00 O ATOM 6157 O HOH D 59 71.979 39.579 3.981 1.00 20.00 O ATOM 6158 O HOH D 60 45.682 29.099 −47.872 1.00 20.00 O ATOM 6159 O HOH D 61 71.067 30.868 −5.015 1.00 20.00 O ATOM 6160 O HOH D 62 60.659 18.305 −24.281 1.00 20.00 O ATOM 6161 O HOH D 63 44.359 21.281 −42.863 1.00 20.00 O ATOM 6162 O HOH D 64 57.959 55.697 −57.920 1.00 20.00 O ATOM 6163 O HOH D 65 58.446 52.296 −29.595 1.00 20.00 O ATOM 6164 O HOH D 66 67.212 38.841 −4.900 1.00 20.00 O ATOM 6165 O HOH D 67 71.061 42.887 4.621 1.00 20.00 O ATOM 6166 O HOH D 68 72.173 47.222 −18.486 1.00 20.00 O ATOM 6167 O HOH D 69 61.180 29.465 6.359 1.00 20.00 O ATOM 6168 O HOH D 70 53.686 19.114 −17.263 1.00 20.00 O ATOM 6169 O HOH D 71 94.324 10.514 −22.199 1.00 20.00 O ATOM 6170 O HOH D 72 71.727 30.019 1.431 1.00 20.00 O ATOM 6171 O HOH D 73 68.203 22.419 −44.523 1.00 20.00 O ATOM 6172 O HOH D 74 86.700 43.770 −10.866 1.00 20.00 O ATOM 6173 O HOH D 75 49.053 1.930 −4.743 1.00 20.00 O ATOM 6174 O HOH D 76 48.953 41.469 −35.852 1.00 20.00 O ATOM 6175 O HOH D 77 82.324 43.914 −3.552 1.00 20.00 O ATOM 6176 O HOH D 78 61.390 31.895 −61.735 1.00 20.00 O ATOM 6177 O HOH D 79 54.422 21.537 −25.218 1.00 20.00 O ATOM 6178 O HOH D 80 60.649 30.670 −2.107 1.00 20.00 O ATOM 6179 O HOH D 81 57.672 45.977 −12.143 1.00 20.00 O ATOM 6180 O HOH D 82 65.179 40.572 −36.435 1.00 20.00 O ATOM 6181 O HOH D 83 59.030 29.360 −26.403 1.00 20.00 O ATOM 6182 O HOH D 84 56.594 22.155 10.811 1.00 20.00 O ATOM 6183 O HOH D 85 65.436 43.103 −27.013 1.00 20.00 O ATOM 6184 O HOH D 86 89.907 6.442 −2.810 1.00 20.00 O ATOM 6185 O HOH D 87 70.388 24.868 −42.470 1.00 20.00 O ATOM 6186 O HOH D 88 58.020 10.532 −3.262 1.00 20.00 O ATOM 6187 O HOH D 89 77.585 19.803 −24.675 1.00 20.00 O ATOM 6188 O HOH D 90 68.516 44.759 −75.007 1.00 20.00 O ATOM 6189 O HOH D 91 65.211 29.187 −55.944 1.00 20.00 O ATOM 6190 O HOH D 92 75.807 68.071 −44.741 1.00 20.00 O ATOM 6191 O HOH D 93 57.689 41.210 −30.041 1.00 20.00 O ATOM 6192 O HOH D 94 43.896 2.084 −10.290 1.00 20.00 O ATOM 6193 O HOH D 95 84.660 25.547 −5.453 1.00 20.00 O ATOM 6194 O HOH D 96 60.499 75.473 −31.924 1.00 20.00 O ATOM 6195 O HOH D 97 60.009 48.578 −76.553 1.00 20.00 O ATOM 6196 O HOH D 98 76.515 36.746 −40.808 1.00 20.00 O ATOM 6197 O HOH D 99 64.802 12.673 −21.721 1.00 20.00 O ATOM 6198 O HOH D 100 82.399 26.386 −39.626 1.00 20.00 O ATOM 6199 O HOH D 101 70.077 35.468 −28.982 1.00 20.00 O ATOM 6200 O HOH D 102 52.710 55.450 −32.808 1.00 20.00 O ATOM 6201 O HOH D 103 59.976 2.969 −12.580 1.00 20.00 O ATOM 6202 O HOH D 104 86.802 41.783 −36.452 1.00 20.00 O ATOM 6203 O HOH D 105 84.149 27.273 −13.597 1.00 20.00 O ATOM 6204 O HOH D 106 71.556 29.575 −2.196 1.00 20.00 O ATOM 6205 O HOH D 107 51.264 52.557 −49.022 1.00 20.00 O ATOM 6206 O HOH D 108 75.268 65.764 −28.610 1.00 20.00 O ATOM 6207 O HOH D 109 82.562 14.795 −24.801 1.00 20.00 O ATOM 6208 O HOH D 110 50.132 18.739 −52.640 1.00 20.00 O ATOM 6209 O HOH D 111 71.354 24.987 −36.642 1.00 20.00 O ATOM 6210 O HOH D 112 45.114 32.720 −52.267 1.00 20.00 O ATOM 6211 O HOH D 113 48.420 0.249 −2.315 1.00 20.00 O ATOM 6212 O HOH D 114 63.390 16.967 −37.223 1.00 20.00 O ATOM 6213 O HOH D 115 44.699 36.738 −43.228 1.00 20.00 O ATOM 6214 O HOH D 116 56.574 71.854 −54.993 1.00 20.00 O ATOM 6215 O HOH D 117 53.797 60.299 −41.403 1.00 20.00 O ATOM 6216 O HOH D 118 46.104 2.883 0.638 1.00 20.00 O ATOM 6217 O HOH D 119 53.543 28.997 −9.765 1.00 20.00 O ATOM 6218 O HOH D 120 72.241 43.861 −26.923 1.00 20.00 O ATOM 6219 O HOH D 121 63.247 65.191 −20.060 1.00 20.00 O ATOM 6220 O HOH D 122 45.329 19.594 −13.586 1.00 20.00 O ATOM 6221 O HOH D 123 64.023 26.710 −49.259 1.00 20.00 O ATOM 6222 O HOH D 124 48.910 41.318 −22.753 1.00 20.00 O ATOM 6223 O HOH D 125 82.532 60.598 −36.480 1.00 20.00 O ATOM 6224 O HOH D 126 67.063 13.897 −30.167 1.00 20.00 O ATOM 6225 O HOH D 127 50.361 40.065 −56.024 1.00 20.00 O ATOM 6226 O HOH D 128 72.976 45.157 −4.246 1.00 20.00 O ATOM 6227 O HOH D 129 75.216 64.672 −53.791 1.00 20.00 O ATOM 6228 O HOH D 130 65.468 10.968 −15.412 1.00 20.00 O ATOM 6229 O HOH D 131 51.343 68.145 −32.846 1.00 20.00 O ATOM 6230 O HOH D 132 56.280 52.648 −67.213 1.00 20.00 O ATOM 6231 O HOH D 133 56.735 56.430 −23.538 1.00 20.00 O ATOM 6232 O HOH D 134 60.995 39.033 −31.591 1.00 20.00 O ATOM 6233 O HOH D 135 89.055 32.196 −5.724 1.00 20.00 O ATOM 6234 O HOH D 136 72.037 50.093 −76.504 1.00 20.00 O ATOM 6235 O HOH D 137 58.047 16.908 −24.405 1.00 20.00 O ATOM 6236 O HOH D 138 77.131 28.831 −4.157 1.00 20.00 O ATOM 6237 O HOH D 139 77.050 −0.539 −22.670 1.00 20.00 O ATOM 6238 O HOH D 140 49.237 43.219 −19.100 1.00 20.00 O ATOM 6239 O HOH D 141 51.363 54.581 −35.081 1.00 20.00 O ATOM 6240 O HOH D 142 60.768 12.246 3.533 1.00 20.00 O ATOM 6241 O HOH D 143 82.143 33.605 −11.456 1.00 20.00 O ATOM 6242 O HOH D 144 84.866 34.019 −4.279 1.00 20.00 O ATOM 6243 O HOH D 145 46.907 21.739 −20.630 1.00 20.00 O ATOM 6244 O HOH D 146 63.588 51.236 −61.514 1.00 20.00 O ATOM 6245 O HOH D 147 76.048 26.901 −8.051 1.00 20.00 O ATOM 6246 O HOH D 148 75.152 17.176 −9.502 1.00 20.00 O ATOM 6247 O HOH D 149 53.908 49.543 −48.224 1.00 20.00 O ATOM 6248 O HOH D 150 55.904 34.679 −28.831 1.00 20.00 O ATOM 6249 O HOH D 151 82.610 13.849 −0.078 1.00 20.00 O ATOM 6250 O HOH D 152 66.977 30.695 −54.273 1.00 20.00 O ATOM 6251 O HOH D 153 66.841 35.486 −1.504 1.00 20.00 O ATOM 6252 O HOH D 154 82.757 34.137 3.334 1.00 20.00 O ATOM 6253 O HOH D 155 54.147 9.570 3.284 1.00 20.00 O ATOM 6254 O HOH D 156 80.578 41.318 −34.825 1.00 20.00 O ATOM 6255 O HOH D 157 63.302 21.304 −5.676 1.00 20.00 O ATOM 6256 O HOH D 158 64.938 71.646 −51.103 1.00 20.00 O ATOM 6257 O HOH D 159 95.142 46.020 −17.820 1.00 20.00 O ATOM 6258 O HOH D 160 75.645 45.515 −4.504 1.00 20.00 O ATOM 6259 O HOH D 161 49.971 51.159 −51.013 1.00 20.00 O ATOM 6260 O HOH D 162 46.062 62.230 −35.071 1.00 20.00 O ATOM 6261 O HOH D 163 64.042 23.147 3.695 1.00 20.00 O ATOM 6262 O HOH D 164 54.456 56.856 −17.260 1.00 20.00 O ATOM 6263 O HOH D 165 80.892 59.070 −39.373 1.00 20.00 O ATOM 6264 O HOH D 166 78.713 27.343 −17.177 1.00 20.00 O ATOM 6265 O HOH D 167 56.338 42.558 −38.635 1.00 20.00 O ATOM 6266 O HOH D 168 81.550 66.121 −39.390 1.00 20.00 O ATOM 6267 O HOH D 169 76.949 −1.075 −9.319 1.00 20.00 O ATOM 6268 O HOH D 170 54.280 63.938 −61.226 1.00 20.00 O ATOM 6269 O HOH D 171 48.871 55.989 −32.767 1.00 20.00 O ATOM 6270 O HOH D 172 44.127 41.159 −37.268 1.00 20.00 O ATOM 6271 O HOH D 173 73.358 23.594 −6.296 1.00 20.00 O ATOM 6272 O HOH D 174 83.332 40.334 3.740 1.00 20.00 O ATOM 6273 O HOH D 175 57.456 61.840 −28.946 1.00 20.00 O ATOM 6274 O HOH D 176 47.864 39.468 −52.196 1.00 20.00 O ATOM 6275 O HOH D 177 70.906 44.639 −40.681 1.00 20.00 O ATOM 6276 O HOH D 178 47.058 37.463 −50.633 1.00 20.00 O ATOM 6277 O HOH D 179 86.981 6.334 −19.280 1.00 20.00 O ATOM 6278 O HOH D 180 44.628 56.126 −34.042 1.00 20.00 O ATOM 6279 O HOH D 181 83.980 53.458 −40.071 1.00 20.00 O ATOM 6280 O HOH D 182 59.166 73.532 −46.016 1.00 20.00 O ATOM 6281 O HOH D 183 77.303 44.139 0.829 1.00 20.00 O ATOM 6282 O HOH D 184 80.642 24.436 −31.825 1.00 20.00 O ATOM 6283 O HOH D 185 43.385 53.300 −33.516 1.00 20.00 O ATOM 6284 O HOH D 186 62.566 23.618 1.479 1.00 20.00 O ATOM 6285 O HOH D 187 73.669 57.702 −22.905 1.00 20.00 O ATOM 6286 O HOH D 188 49.415 59.473 −24.944 1.00 20.00 O ATOM 6287 O HOH D 189 71.810 61.853 −59.613 1.00 20.00 O ATOM 6288 O HOH D 190 62.070 57.486 −19.683 1.00 20.00 O ATOM 6289 O HOH D 191 56.953 67.436 −60.936 1.00 20.00 O ATOM 6290 O HOH D 192 82.033 55.372 −41.403 1.00 20.00 O ATOM 6291 O HOH D 193 47.622 44.222 −37.928 1.00 20.00 O ATOM 6292 O HOH D 194 45.429 32.478 −56.159 1.00 20.00 O ATOM 6293 O HOH D 195 44.089 24.893 −38.558 1.00 20.00 O ATOM 6294 O HOH D 196 87.459 2.740 −23.712 1.00 20.00 O ATOM 6295 O HOH D 197 43.461 21.812 −12.797 1.00 20.00 O ATOM 6296 O HOH D 198 53.724 41.172 −56.872 1.00 20.00 O ATOM 6297 O HOH D 199 90.493 44.361 −31.343 1.00 20.00 O ATOM 6298 O HOH D 200 62.530 47.992 −18.654 1.00 20.00 O ATOM 6299 O HOH D 201 105.952 13.181 −18.288 1.00 20.00 O ATOM 6300 O HOH D 202 64.012 47.558 −47.893 1.00 20.00 O ATOM 6301 O HOH D 203 71.648 19.923 −53.444 1.00 20.00 O ATOM 6302 O HOH D 204 57.867 9.549 8.360 1.00 20.00 O ATOM 6303 O HOH D 205 67.895 29.061 11.145 1.00 20.00 O ATOM 6304 O HOH D 206 46.864 2.022 −10.737 1.00 20.00 O ATOM 6305 O HOH D 207 72.344 41.871 −60.207 1.00 20.00 O ATOM 6306 O HOH D 208 76.428 69.471 −39.044 1.00 20.00 O ATOM 6307 O HOH D 209 66.747 25.420 −54.664 1.00 20.00 O ATOM 6308 O HOH D 210 93.795 50.023 −36.541 1.00 20.00 O ATOM 6309 O HOH D 211 78.065 66.179 −41.924 1.00 20.00 O ATOM 6310 O HOH D 212 76.175 17.753 −23.518 1.00 20.00 O ATOM 6311 O HOH D 213 86.703 56.266 −23.536 1.00 20.00 O ATOM 6312 O HOH D 214 65.986 14.564 3.742 1.00 20.00 O ATOM 6313 O HOH D 215 98.725 3.513 −17.143 1.00 20.00 O ATOM 6314 O HOH D 216 79.130 26.874 −19.954 1.00 20.00 O ATOM 6315 O HOH D 217 49.317 53.293 −46.497 1.00 20.00 O ATOM 6316 O HOH D 218 90.903 5.188 −21.891 1.00 20.00 O ATOM 6317 O HOH D 219 62.347 40.747 −30.721 1.00 20.00 O ATOM 6318 O HOH D 220 40.643 60.376 −62.136 1.00 20.00 O ATOM 6319 O HOH D 221 71.503 54.166 −54.497 1.00 20.00 O ATOM 6320 O HOH D 222 44.805 23.084 −40.706 1.00 20.00 O ATOM 6321 O HOH D 223 51.651 36.116 −28.720 1.00 20.00 O ATOM 6322 O HOH D 224 59.269 20.776 3.522 1.00 20.00 O ATOM 6323 O HOH D 225 77.291 19.357 −18.420 1.00 20.00 O ATOM 6324 O HOH D 226 44.413 54.785 −38.531 1.00 20.00 O ATOM 6325 O HOH D 227 90.231 4.458 −4.698 1.00 20.00 O ATOM 6326 O HOH D 228 43.333 12.575 3.377 1.00 20.00 O ATOM 6327 O HOH D 229 44.195 19.482 0.211 1.00 20.00 O ATOM 6328 O HOH D 230 69.638 22.262 −38.599 1.00 20.00 O ATOM 6329 O HOH D 231 47.271 22.934 −17.869 1.00 20.00 O ATOM 6330 O HOH D 232 45.447 36.954 −39.399 1.00 20.00 O ATOM 6331 O HOH D 233 77.160 62.378 −49.290 1.00 20.00 O ATOM 6332 O HOH D 234 71.208 33.921 2.980 1.00 20.00 O ATOM 6333 O HOH D 235 52.702 27.857 −26.436 1.00 20.00 O ATOM 6334 O HOH D 236 56.489 22.551 14.990 1.00 20.00 O ATOM 6335 O HOH D 237 88.130 58.148 −22.506 1.00 20.00 O ATOM 6336 O HOH D 238 56.698 27.605 −26.317 1.00 20.00 O ATOM 6337 O HOH D 239 56.912 45.842 −9.201 1.00 20.00 O ATOM 6338 O HOH D 240 65.448 9.613 −21.628 1.00 20.00 O ATOM 6339 O HOH D 241 46.950 18.587 1.252 1.00 20.00 O ATOM 6340 O HOH D 242 69.391 27.146 −54.199 1.00 20.00 O ATOM 6341 O HOH D 243 50.184 17.922 0.936 1.00 20.00 O ATOM 6342 O HOH D 244 70.148 41.168 −42.647 1.00 20.00 O END

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1. A method of designing a modulator of a myosin, the method comprising molecular modeling of a compound such that the modeled compound interacts with at least three amino acid residues of said myosin, said residues being selected from (a) ranges K265-V268, V411-L441, N588-Q593, D614-T629, and V630-E646 of SEQ ID NO: 2, said myosin comprising or consisting of (i) the sequence of SEQ ID NO: 2; (ii) the sequence encoded by the sequence of SEQ ID NO: 1; (iii) a sequence being at least 40% identical to the sequence of SEQ ID NO: 2 or to the sequence encoded by the sequence of SEQ ID NO: 1; or (iv) a sequence encoded by a sequence being at least 40% identical to the sequence of SEQ ID NO: 1; wherein said sequence of (iii) or (iv) comprises said three amino acid residues, and wherein said residues comprise K265; or (b) ranges of any one of SEQ ID NOs: 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, 80, 82, 84, 86, 88, 90, 92, 94, 96, 98, 100, 102, 104, 106 or 108, respectively, said ranges aligning with the ranges of SEQ ID NO: 2 as defined in (a), said myosin comprising or consisting of (i) the sequence of any one of SEQ ID NO: 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, 80, 82, 84, 86, 88, 90, 92, 94, 96, 98, 100, 102, 104, 106 or 108, respectively; (ii) the sequence encoded by the sequence of any one of SEQ ID NO: 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, 47, 49, 51, 53, 55, 57, 59, 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, 81, 83, 85, 87, 89, 91, 93, 95, 97, 99, 101, 103, 105, 107 or 109, respectively; (iii) a sequence being at least 40% identical to the sequence of any one of SEQ ID NO: 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, 80, 82, 84, 86, 88, 90, 92, 94, 96, 98, 100, 102, 104, 106 or 108, respectively, or to the sequence encoded by the sequence of any one of SEQ ID NO: 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, 47, 49, 51, 53, 55, 57, 59, 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, 81, 83, 85, 87, 89, 91, 93, 95, 97, 99, 101, 103, 105, 107 or 109, respectively; or (iv) a sequence encoded by a sequence being at least 40% identical to the sequence of any one of SEQ ID NO: 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, 47, 49, 51, 53, 55, 57, 59, 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, 81, 83, 85, 87, 89, 91, 93, 95, 97, 99, 101, 103, 105, 107 or 109, respectively; wherein said sequence of (iii) or (iv) comprises said three amino acid residues, and wherein said residues comprise the residue aligning with K265 of SEQ ID NO: 2; thereby obtaining said modulator of a myosin.
 2. The method of claim 1, further comprising synthesizing said modulator, thereby producing said modulator.
 3. The method of claim 1 or 2, wherein said molecular modeling comprises (i) measuring at least one intermolecular distance; and/or (ii) calculating at least one free energy of interaction.
 4. The method of any one of claims 1 to 3, wherein said ranges as defined in claim 1 (a) are limited to the following positions: K265, A420, K423, A424, R428, L431, D590, I617, and A618.
 5. A method of identifying a modulator of a myosin, the method comprising (a) bringing into contact a myosin and a test compound; (b) determining whether said test compound interacts with at least three amino acid residues selected from (ba) ranges K265-V268, V411-L441, N588-Q593, D614-T629, and V630-E646 of SEQ ID NO: 2, said myosin comprising or consisting of (i) the sequence of SEQ ID NO: 2; (ii) the sequence encoded by the sequence of SEQ ID NO: 1; (iii) a sequence being at least 40% identical to the sequence of SEQ ID NO: 2 or to the sequence encoded by the sequence of SEQ ID NO: 1; or (iv) a sequence encoded by a sequence being at least 40% identical to the sequence of SEQ ID NO: 1; wherein said sequence of (iii) or (iv) comprises said three amino acid residues, and wherein said residues comprise K265; or (bb) ranges of any one of SEQ ID NOs: 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, 80, 82, 84, 86, 88, 90, 92, 94, 96, 98, 100, 102, 104, 106 or 108, respectively, said ranges aligning with the ranges of SEQ ID NO: 2 as defined in (a), said myosin comprising or consisting of (i) the sequence of any one of SEQ ID NO: 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, 80, 82, 84, 86, 88, 90, 92, 94, 96, 98, 100, 102, 104, 106 or 108, respectively; (ii) the sequence encoded by the sequence of any one of SEQ ID NO: 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, 47, 49, 51, 53, 55, 57, 59, 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, 81, 83, 85, 87, 89, 91, 93, 95, 97, 99, 101, 103, 105, 107 or 109, respectively; (iii) a sequence being at least 40% identical to the sequence of any one of SEQ ID NO: 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 36, 38, 40, 42, 44, 46, 48, 50, 52, 54, 56, 58, 60, 62, 64, 66, 68, 70, 72, 74, 76, 78, 80, 82, 84, 86, 88, 90, 92, 94, 96, 98, 100, 102, 104, 106 or 108, respectively, or to the sequence encoded by the sequence of any one of SEQ ID NO: 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, 47, 49, 51, 53, 55, 57, 59, 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, 81, 83, 85, 87, 89, 91, 93, 95, 97, 99, 101, 103, 105, 107 or 109, respectively; or (iv) a sequence encoded by a sequence being at least 40% identical to the sequence of any one of SEQ ID NO: 3, 5, 7, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29, 31, 33, 35, 37, 39, 41, 43, 45, 47, 49, 51, 53, 55, 57, 59, 61, 63, 65, 67, 69, 71, 73, 75, 77, 79, 81, 83, 85, 87, 89, 91, 93, 95, 97, 99, 101, 103, 105, 107 or 109, respectively; wherein said sequence of (iii) or (iv) comprises said three amino acid residues, and wherein said residues comprise the residue aligning with K265 of SEQ ID NO: 2; and (c) identifying those compounds which interact with said at least three amino acid residues, thereby identifying said modulator of a myosin.
 6. The method of claim 5, wherein said determining in step (b) is effected by X-ray crystallography and/or NMR spectroscopy.
 7. The method of claim 5 or 6, further comprising the step of (a′) (i) determining whether said test compound binds to said myosin; and/or (ii) determining whether said test compound modulates the activity and/or conformation of said myosin; and/or (iii) determining the cytotoxicity of said test compound; wherein step (a) is to be effected after step (a) and prior to step (b), and wherein said determining in step (b) is performed with test compounds determined to bind, to modulate, and/or to be cytotoxic in step (a′).
 8. The method of claim 7, wherein said activity is the capability of said myosin (i) to bind actin; (ii) to convert ATP into ADP and P_(i); and/or (iii) to generate force and/or movement.
 9. The method of any one of the preceding claims, wherein molecular modeling according to any one of claims 1 to 3 starts from a compound selected from compounds of the general formulae (1) to (4) or a salt or solvate thereof, or the test compound of any one of claims 4 to 7 is selected from compounds of the general formulae (1) to (4) or a salt or solvate thereof

wherein X is selected from NH, O and S; and Y and Z designate, as valence permits, one or more substituents, wherein each occurrence of Y and Z is independently selected from F, Cl, Br, I, R and OR; R being selected from (i) H, (ii) (CO)CH₃, and (iii) linear or branched alkyl, alkenyl or alkinyl with one to four carbon atoms, the moieties (ii) and (iii) being optionally substituted with one or more F, Cl, Br and/or I.
 10. Use of a compound selected from compounds of the general formulae (1) to (4) or a salt or solvate thereof as a lead compound in the development of a modulator of a myosin.
 11. The method of claim 9 or the use of claim 10, wherein said general formulae are the general formulae (1) or (2).
 12. The method of any one of claim 1 to 9 or 11, or the use of claim 10 or 11, wherein said modulator is an inhibitor.
 13. A pharmaceutical composition comprising one or more compounds selected from compounds of the general formulae (1), (2) and (4) as defined in claim 9; 2,3,4-tribromo-5-(1′-methoxy-2′,4′-difluoro-phenyl)-pyrrol; and the compounds shown below, wherein CF₃ may replace one, more or all occurrences of F, Cl, Br and/or MeO in said compounds shown below:

or a salt or solvate thereof.
 14. Use of one or more compounds as defined in claim 13 for the manufacture a pharmaceutical composition for the treatment and/or prevention of cardiovascular diseases, cancer, diseases of the central nervous system, viral infections, and infections by parasites of the Apicomplexa family.
 15. A compound of the following formula A-L-B, wherein A is selected from compounds of the general formulae (1) to (4) as defined in claim 9, L is a linker, B is blebbistatin or an analogue thereof, and “—” is a covalent bond.
 16. The pharmaceutical composition of claim 13, the use of claim 14, or the compound of claim 15, wherein said one or more compounds of claim 13 or 14 or the compound A of claim 15 are selected from compounds of the formulae (1′), (2′) and (3′):

wherein Y₁, Y₂, Y₃, Y₄, Y₅, Y₆, and Y₇ are independently selected from H, F, Cl, Br, I, R and OR; R being selected from (i) H, (ii) (CO)CH₃, and (iii) linear or branched alkyl, alkenyl or alkinyl with one to four carbon atoms, optionally substituted with one or more F, Cl, Br and/or I; or a salt or solvate thereof.
 17. The pharmaceutical composition, the use, or the compound of claim 16, wherein (i) Y₁, Y₄ and Y₆ of formula (1′) are H; and/or (ii) Y₁, Y₄, Y₆ and Y₇ of formula (2′) are H.
 18. The pharmaceutical composition, the use, or the compound of claim 17, wherein furthermore (i) Y₇ of formula (1′) is H; and/or (ii) Y₂ of formula (2′) is H. 